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Search results 301 to 328 out of 328 for Lbh

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0.017s

Type

Details

Score

Publication

15843621 | J:145979

First Author:	Segal JP
Year:	2005
Journal:	J Neurosci
Title:	Use of laser-capture microdissection for the identification of marker genes for the ventromedial hypothalamic nucleus.
Volume:	25
Issue:	16
Pages:	4181-8

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Publication

9012664 | -

First Author:	Beaman TW
Year:	1997
Journal:	Biochemistry
Title:	Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Volume:	36
Issue:	3
Pages:	489-94

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Protein Domain

IPR005664 | DapD_Trfase_Hexpep_rpt_fam

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.

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Publication

7814319 | -

First Author:	Annunziato PW
Year:	1995
Journal:	J Bacteriol
Title:	Nucleotide sequence and genetic analysis of the neuD and neuB genes in region 2 of the polysialic acid gene cluster of Escherichia coli K1.
Volume:	177
Issue:	2
Pages:	312-9

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Publication

16490781 | -

First Author:	Lewis AL
Year:	2006
Journal:	J Biol Chem
Title:	The group B streptococcal sialic acid O-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters.
Volume:	281
Issue:	16
Pages:	11186-92

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Publication

16923886 | -

First Author:	Steenbergen SM
Year:	2006
Journal:	J Bacteriol
Title:	Separate pathways for O acetylation of polymeric and monomeric sialic acids and identification of sialyl O-acetyl esterase in Escherichia coli K1.
Volume:	188
Issue:	17
Pages:	6195-206

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Publication

18201574 | -

First Author:	Albermann C
Year:	2008
Journal:	FEBS Lett
Title:	Identification of the GDP-N-acetyl-d-perosamine producing enzymes from Escherichia coli O157:H7.
Volume:	582
Issue:	4
Pages:	479-84

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Publication

19448740 | -

First Author:	Demendi M
Year:	2009
Journal:	Biochem Cell Biol
Title:	Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni.
Volume:	87
Issue:	3
Pages:	469-83

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Publication

17087520 | -

First Author:	Olivier NB
Year:	2006
Journal:	Biochemistry
Title:	In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system.
Volume:	45
Issue:	45
Pages:	13659-69

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Publication

15500694 | -

First Author:	Parisi G
Year:	2004
Journal:	BMC Evol Biol
Title:	The structurally constrained protein evolution model accounts for sequence patterns of the LbetaH superfamily.
Volume:	4

Pages:	41

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Protein Domain

IPR020019 | Sia_OAcTrfase_NeuD-like

Type:

Family

Description:

This entry includes a group of acetyltransferases, such as NeuD sialic acid O-acetyltransferase enzymes from Escherichia coli and Streptococcus agalactiae (group B strep) [, , ], UDP-N-acetylbacillosamine N-acetyltransferase pglD from Campylobacter jejuni subsp. jejuni [, ]and GDP-perosamine N-acetyltransferase perB from Escherichia coli O157:H7 []. This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV].-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity [].The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) has not been demonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA itself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differing sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis.

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Publication

11910040 | -

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

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Publication

20436479 | J:157819

First Author:	Shimogori T
Year:	2010
Journal:	Nat Neurosci
Title:	A genomic atlas of mouse hypothalamic development.
Volume:	13
Issue:	6
Pages:	767-75

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Publication

20418392 | -

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

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Publication

11352712 | -

First Author:	Viola RE
Year:	2001
Journal:	Acc Chem Res
Title:	The central enzymes of the aspartate family of amino acid biosynthesis.
Volume:	34
Issue:	5
Pages:	339-49

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Publication

15345747 | -

First Author:	Ballif BA
Year:	2004
Journal:	Mol Cell Proteomics
Title:	Phosphoproteomic analysis of the developing mouse brain.
Volume:	3
Issue:	11
Pages:	1093-101

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Publication

- | J:84900

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2003
Journal:	Database Download
Title:	Integrating Computational Gene Models into the Mouse Genome Informatics (MGI) Database

•

Publication

18799693 | J:142754

First Author:	Hansen GM
Year:	2008
Journal:	Genome Res
Title:	Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume:	18
Issue:	10
Pages:	1670-9

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Publication

- | J:73796

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2002

Title:	Function or Process or Component Unknown following Literature Review

•

Publication

14610273 | J:86696

First Author:	Zambrowicz BP
Year:	2003
Journal:	Proc Natl Acad Sci U S A
Title:	Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume:	100
Issue:	24
Pages:	14109-14

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Publication

16141072 | J:99680

First Author:	Carninci P
Year:	2005
Journal:	Science
Title:	The transcriptional landscape of the mammalian genome.
Volume:	309
Issue:	5740
Pages:	1559-63

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Publication

- | J:141210

First Author:	Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year:	2008
Journal:	Database Download
Title:	Mouse Gene Trap Data Load from dbGSS

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Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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Publication

- | J:23000

First Author:	MGD Nomenclature Committee
Year:	1995

Title:	Nomenclature Committee Use

•

Publication

21267068 | J:153498

First Author:	Diez-Roux G
Year:	2011
Journal:	PLoS Biol
Title:	A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume:	9
Issue:	1
Pages:	e1000582

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Publication

- | J:75000

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2002

Title:	Mouse Genome Informatics Computational Sequence to Gene Associations

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Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

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Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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