| Type |
Details |
Score |
| Publication |
| First Author: |
Nico B |
| Year: |
2010 |
| Journal: |
Lab Invest |
| Title: |
Glial dystrophin-associated proteins, laminin and agrin, are downregulated in the brain of mdx mouse. |
| Volume: |
90 |
| Issue: |
11 |
| Pages: |
1645-60 |
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•
•
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| Publication |
| First Author: |
Wieneke S |
| Year: |
2003 |
| Journal: |
J Appl Physiol (1985) |
| Title: |
Acute pathophysiological effects of muscle-expressed Dp71 transgene on normal and dystrophic mouse muscle. |
| Volume: |
95 |
| Issue: |
5 |
| Pages: |
1861-6 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Rafael JA |
| Year: |
1996 |
| Journal: |
J Cell Biol |
| Title: |
Forced expression of dystrophin deletion constructs reveals structure-function correlations. |
| Volume: |
134 |
| Issue: |
1 |
| Pages: |
93-102 |
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•
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•
•
|
| Publication |
| First Author: |
Yang B |
| Year: |
1994 |
| Journal: |
J Biol Chem |
| Title: |
Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression. |
| Volume: |
269 |
| Issue: |
8 |
| Pages: |
6040-4 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Hoddevik EH |
| Year: |
2020 |
| Journal: |
Brain Struct Funct |
| Title: |
Organisation of extracellular matrix proteins laminin and agrin in pericapillary basal laminae in mouse brain. |
| Volume: |
225 |
| Issue: |
2 |
| Pages: |
805-816 |
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•
•
•
•
|
| Publication |
| First Author: |
Imamura M |
| Year: |
2005 |
| Journal: |
Hum Mol Genet |
| Title: |
Epsilon-sarcoglycan compensates for lack of alpha-sarcoglycan in a mouse model of limb-girdle muscular dystrophy. |
| Volume: |
14 |
| Issue: |
6 |
| Pages: |
775-83 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Lee H |
| Year: |
2022 |
| Journal: |
Front Cell Dev Biol |
| Title: |
Tissue-specific requirement of sodium channel and clathrin linker 1 (Sclt1) for ciliogenesis during limb development. |
| Volume: |
10 |
|
| Pages: |
1058895 |
|
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•
•
•
•
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| Publication |
| First Author: |
Wang Y |
| Year: |
2010 |
| Journal: |
Brain Res |
| Title: |
Flufenamic acid modulates multiple currents in gonadotropin-releasing hormone neurons. |
| Volume: |
1353 |
|
| Pages: |
94-105 |
|
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•
•
•
•
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| Publication |
| First Author: |
Khattar NH |
| Year: |
1997 |
| Journal: |
Somat Cell Mol Genet |
| Title: |
A role for certain mouse Aprt sequences in resistance to toxic adenine analogs. |
| Volume: |
23 |
| Issue: |
1 |
| Pages: |
51-61 |
|
•
•
•
•
•
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| Publication |
| First Author: |
Yoshida M |
| Year: |
2000 |
| Journal: |
Hum Mol Genet |
| Title: |
Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy. |
| Volume: |
9 |
| Issue: |
7 |
| Pages: |
1033-40 |
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•
•
•
•
|
| Publication |
| First Author: |
Sakagami H |
| Year: |
1997 |
| Journal: |
Brain Res Mol Brain Res |
| Title: |
Molecular cloning and developmental expression of a rat homologue of death-associated protein kinase in the nervous system. |
| Volume: |
52 |
| Issue: |
2 |
| Pages: |
249-56 |
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•
•
•
•
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| Publication |
| First Author: |
Kögel D |
| Year: |
1998 |
| Journal: |
Oncogene |
| Title: |
Cloning and characterization of Dlk, a novel serine/threonine kinase that is tightly associated with chromatin and phosphorylates core histones. |
| Volume: |
17 |
| Issue: |
20 |
| Pages: |
2645-54 |
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•
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•
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| Publication |
| First Author: |
Zhang X |
| Year: |
2012 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Identification of a tetratricopeptide repeat-like domain in the nicastrin subunit of γ-secretase using synthetic antibodies. |
| Volume: |
109 |
| Issue: |
22 |
| Pages: |
8534-9 |
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•
•
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| Publication |
| First Author: |
Fuchs TM |
| Year: |
2000 |
| Journal: |
J Bacteriol |
| Title: |
Characterization of a bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-succinyl-L,L-DAP aminotransferase. |
| Volume: |
182 |
| Issue: |
13 |
| Pages: |
3626-31 |
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•
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•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents the diaminopimelate dehydrogenase enzyme which provides an alternate (shortcut) route of lysine biosynthesis in Corynebacterium, Bacterioides, Porphyromonas and other species. The enzyme from Corynebacterium glutamicum (Brevibacterium flavum) has been crystallized and characterised []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This family of succinyldiaminopimelate transaminases (DapC) includes the experimentally characterised enzyme from Bordetella pertussis []. The majority of genes in this family are proximal to genes encoding components of the lysine biosynthesis via succinylase diaminopimelate pathway () []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents acetyldiaminopimelate deacetylase, which converts N-acetyl-L-2-amino-6-diaminopimelate to L,L-DAP. It is the last step of the lysine biosynthesis acetylase pathway. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Liu Y |
| Year: |
2010 |
| Journal: |
J Bacteriol |
| Title: |
Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis. |
| Volume: |
192 |
| Issue: |
13 |
| Pages: |
3304-10 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wehrmann A |
| Year: |
1994 |
| Journal: |
Microbiology |
| Title: |
Analysis of different DNA fragments of Corynebacterium glutamicum complementing dapE of Escherichia coli. |
| Volume: |
140 ( Pt 12) |
|
| Pages: |
3349-56 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Scapin G |
| Year: |
1996 |
| Journal: |
Biochemistry |
| Title: |
Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. |
| Volume: |
35 |
| Issue: |
42 |
| Pages: |
13540-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang W |
| Year: |
2008 |
| Journal: |
J Am Chem Soc |
| Title: |
Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. |
| Volume: |
130 |
| Issue: |
19 |
| Pages: |
6068-9 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Návarová H |
| Year: |
2012 |
| Journal: |
Plant Cell |
| Title: |
Pipecolic acid, an endogenous mediator of defense amplification and priming, is a critical regulator of inducible plant immunity. |
| Volume: |
24 |
| Issue: |
12 |
| Pages: |
5123-41 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC Gram-positives) and is based on the characterisation of the enzyme from Corynebacterium glutamicum (Brevibacterium flavum) []. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases. They are classified as non-peptidases homologues belonging to MEROPS peptidase family M20A |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.The four sequences which make up the seed for this model are not closely related, although they are all members of the family of aminotransferases and are more closely related to each other than to anything else. Additionally, all of them are found in the vicinity of genes involved in the biosynthesis of lysine via the diaminopimelate pathway (), although this amounts to a separation of 12 genes in the case of Sulfurihydrogenibium azorense Az-Fu1. None of these genomes contain another strong candidate for this role in the pathway. Note: the detailed information included in the record includes the assertions that the enzyme uses the pyridoxal pyrophosphate cofactor, which is consistent with the family, and the assertion that the amino group donor is L-glutamate, which is undetermined for the sequences in this clade. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This group of the superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (). Every member of this group is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known aminotransferases, succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh). Although there is no experimental characterisation of any of the sequences in this group, a direct pathway is known in plants and Chlamydia [, ]so it seems quite reasonable that these enzymes catalyse the same transformation. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry includes LL-diaminopimelate aminotransferase DapL from bacteria and aminotransferase ALD1 from plants. DapL is involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. This enzyme catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli. It is also able to use meso-diaminopimelate, cystathionine, lysine or ornithine as substrates []. ALD1 is involved in the biosynthesis of pipecolate (Pip), a metabolite that orchestrates defense amplification, positive regulation of SA biosynthesis, and priming to guarantee effective local resistance induction and the establishment of SAR [, ]. |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This family of actinobacterial proteins are involved in the biosynthesis of the tetracycline antibiotic, oxytetracycline. The minimum set of enzymes required for the biosynthesis of anhydrotetracycline, the first intermediate in the synthesis of oxytetracycline, are OxyL, OxyQ, and OxyT. OxyQ catalyzes the conversion of 4-dedimethylamino-4-oxoanhydrotetracycline to yield 4-amino-4-de(dimethylamino)anhydrotetracycline (4-amino-ATC) []. |
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•
•
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|
| Publication |
| First Author: |
Mills DA |
| Year: |
1993 |
| Journal: |
Appl Environ Microbiol |
| Title: |
Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes. |
| Volume: |
59 |
| Issue: |
9 |
| Pages: |
2927-37 |
|
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•
|
| Publication |
| First Author: |
Gokulan K |
| Year: |
2003 |
| Journal: |
J Biol Chem |
| Title: |
Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis. |
| Volume: |
278 |
| Issue: |
20 |
| Pages: |
18588-96 |
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•
•
•
•
|
| Publication |
| First Author: |
McCoy AJ |
| Year: |
2006 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. |
| Volume: |
103 |
| Issue: |
47 |
| Pages: |
17909-14 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kobashi N |
| Year: |
1999 |
| Journal: |
J Biosci Bioeng |
| Title: |
Kinetic and mutation analyses of aspartate kinase from Thermus flavus. |
| Volume: |
87 |
| Issue: |
6 |
| Pages: |
739-45 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kalinowski J |
| Year: |
1991 |
| Journal: |
Mol Microbiol |
| Title: |
Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. |
| Volume: |
5 |
| Issue: |
5 |
| Pages: |
1197-204 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schendel FJ |
| Year: |
1992 |
| Journal: |
Appl Environ Microbiol |
| Title: |
Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp. |
| Volume: |
58 |
| Issue: |
9 |
| Pages: |
2806-14 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kobashi N |
| Year: |
1999 |
| Journal: |
J Bacteriol |
| Title: |
Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid. |
| Volume: |
181 |
| Issue: |
6 |
| Pages: |
1713-8 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Hernándo-Rico V |
| Year: |
2001 |
| Journal: |
Microbiology |
| Title: |
Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'. |
| Volume: |
147 |
| Issue: |
Pt 6 |
| Pages: |
1547-55 |
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•
•
•
•
|
| Publication |
| First Author: |
Tunca S |
| Year: |
2004 |
| Journal: |
Res Microbiol |
| Title: |
Cloning, characterization and heterologous expression of the aspartokinase and aspartate semialdehyde dehydrogenase genes of cephamycin C-producer Streptomyces clavuligerus. |
| Volume: |
155 |
| Issue: |
7 |
| Pages: |
525-34 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cuadrado Y |
| Year: |
2004 |
| Journal: |
Appl Microbiol Biotechnol |
| Title: |
Characterization of the ask-asd operon in aminoethoxyvinylglycine-producing Streptomyces sp. NRRL 5331. |
| Volume: |
64 |
| Issue: |
2 |
| Pages: |
228-36 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gunji Y |
| Year: |
2004 |
| Journal: |
Biosci Biotechnol Biochem |
| Title: |
Characterization of the L-lysine biosynthetic pathway in the obligate methylotroph Methylophilus methylotrophus. |
| Volume: |
68 |
| Issue: |
7 |
| Pages: |
1449-60 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lu JH |
| Year: |
1997 |
| Journal: |
Lett Appl Microbiol |
| Title: |
Site-directed mutagenesis of the aspartokinase gene lysC and its characterization in Brevibacterium flavum. |
| Volume: |
24 |
| Issue: |
3 |
| Pages: |
211-3 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen NY |
| Year: |
1989 |
| Journal: |
J Gen Microbiol |
| Title: |
Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli. |
| Volume: |
135 |
| Issue: |
11 |
| Pages: |
2931-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wehrmann A |
| Year: |
1998 |
| Journal: |
J Bacteriol |
| Title: |
Different modes of diaminopimelate synthesis and their role in cell wall integrity: a study with Corynebacterium glutamicum. |
| Volume: |
180 |
| Issue: |
12 |
| Pages: |
3159-65 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this entry are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides [, , , , , , , , , , ]. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-, arginine- and related substrates can be classified into different familieson the basis of sequence similarity [, ]. One of these families includesornithine decarboxylase (ODC), which catalyses the transformationof ornithine into putrescine; prokaryotic diaminopimelate decarboxylase, which catalyses the conversion of diaminopimelate into lysine; Pseudomonas syringae pv. tabaciprotein, tabA, which is probably involved in tabtoxin biosynthesis andis similar to diaminopimelate decarboxylase; and bacterial and plant biosynthetic argininedecarboxylase, which catalyses the transformation of arginine into agmatine, the first step in putrescine synthesis from arginine.Although these proteins, which are known collectively as group IVdecarboxylases [], probably share a common evolutionary origin, theirlevels of sequence similarity are low, being confined to a few shortconserved regions. These conserved motifs suggest a common structuralarrangement for positioning of substrate and the cofactor pyridoxal5'-phosphate among bacterial diaminopimelate ddecarboxylases, eukaryotic ornithinedecarboxylases and arginine decarboxylases [].This entry represents the diaminopimelate decarboxylase LysA, which converts meso-diaminopimelate into lysine and is the last step of the DAP lysine biosynthetic pathway. The structure of bacterial diaminopimelate decarboxylase has been determined []. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Ding P |
| Year: |
2016 |
| Journal: |
Plant Cell |
| Title: |
Characterization of a Pipecolic Acid Biosynthesis Pathway Required for Systemic Acquired Resistance. |
| Volume: |
28 |
| Issue: |
10 |
| Pages: |
2603-2615 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Beaman TW |
| Year: |
1997 |
| Journal: |
Biochemistry |
| Title: |
Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase. |
| Volume: |
36 |
| Issue: |
3 |
| Pages: |
489-94 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine - in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation in Gram-positive bacteria. Members of the animal kingdom do not posses this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides. For more information see [].Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (also known as tetrahydrodipicolinate N-succinyltransferase or DapD) is part of the succinyl route of of lysine/DAP biosynthesis. The DapD protein is a homotrimer is a trimeric enzyme with each monomer composed of three domain: an N-terminal helical domain, a distinctive left-handed parallel β-helix (LBH) domain, and a predominantly beta C-terminal domain [, ]. The LBH structure is encoded by an imperfect tandem-repeated hexapeptide sequence. Each trimer contains three independent active sites, always occuring at the boundary of two subunits, and formed by residues from one N-terminal domain, one C-terminal domain and two adjacent LBH domains. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine - in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential component of bacterial cell wall biosynthesis, and dipicolinic acid, which is involved in sporulation in Gram-positive bacteria. Members of the animal kingdom do not posses this pathway and must therefore acquire these essential amino acids through their diet. Research into improving the metabolic flux through this pathway has the potential to increase the yield of the essential amino acids in important crops, thus improving their nutritional value. Additionally, since the enzymes are not present in animals, inhibitors of them are promising targets for the development of novel antibiotics and herbicides. For more information see [].Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents diaminopimelate epimerase (), which catalyses the isomerisation of L,L-dimaminopimelate to meso-DAP in the biosynthetic pathway leading from aspartate to lysine. It is a member of the broader family of PLP-independent amino acid racemases. This enzyme is a monomeric protein of about 30kDa consisting of two domains which are homologus in structure though they share little sequence similarity []. Each domain consists of mixed β-sheets which fold into a barrel around the central helix. The active site cleft is formed from both domains and contains two conserved cysteines thought to function as the acid and base in the catalytic reaction []. Other PLP-independent racemases such as glutamate racemase have been shown to share a similar structure and mechanism of catalysis. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Watanabe N |
| Year: |
2007 |
| Journal: |
J Mol Biol |
| Title: |
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. |
| Volume: |
371 |
| Issue: |
3 |
| Pages: |
685-702 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Levy-Strumpf N |
| Year: |
1998 |
| Journal: |
Oncogene |
| Title: |
Death associated proteins (DAPs): from gene identification to the analysis of their apoptotic and tumor suppressive functions. |
| Volume: |
17 |
| Issue: |
25 |
| Pages: |
3331-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sung MH |
| Year: |
1991 |
| Journal: |
J Biol Chem |
| Title: |
Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. |
| Volume: |
266 |
| Issue: |
4 |
| Pages: |
2567-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Beaman TW |
| Year: |
2002 |
| Journal: |
Protein Sci |
| Title: |
Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. |
| Volume: |
11 |
| Issue: |
4 |
| Pages: |
974-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cirilli M |
| Year: |
1998 |
| Journal: |
Biochemistry |
| Title: |
Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. |
| Volume: |
37 |
| Issue: |
47 |
| Pages: |
16452-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lloyd AJ |
| Year: |
2004 |
| Journal: |
Acta Crystallogr D Biol Crystallogr |
| Title: |
Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis. |
| Volume: |
60 |
| Issue: |
Pt 2 |
| Pages: |
397-400 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
425
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
110
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
336
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
318
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Geiser E |
| Year: |
2016 |
| Journal: |
Microb Biotechnol |
| Title: |
Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate. |
| Volume: |
9 |
| Issue: |
1 |
| Pages: |
116-26 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
404
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
502
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
522
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
496
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
424
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
580
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
455
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
424
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
355
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
233
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
156
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
381
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
256
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
496
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
194
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
182
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
166
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
363
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
233
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
374
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
178
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
365
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
432
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Remaut H |
| Year: |
2001 |
| Journal: |
Nat Struct Biol |
| Title: |
Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease. |
| Volume: |
8 |
| Issue: |
8 |
| Pages: |
674-8 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
454
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
416
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
563
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
413
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
430
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
560
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
266
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
402
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
382
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
454
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
416
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
572
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
227
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
278
|
| Fragment?: |
false |
|
•
•
•
•
•
|
