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Search results 301 to 400 out of 414 for Cad

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Type Details Score
Publication
8340392 | J:14199
First Author: Miltenberger RJ
Year: 1993
Journal: J Biol Chem
Title: An inhibitory Raf-1 mutant suppresses expression of a subset of v-raf-activated genes.
Volume: 268
Issue: 21
Pages: 15674-80
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Publication
8573715 | J:29512
First Author: Beck F
Year: 1995
Journal: Dev Dyn
Title: Expression of Cdx-2 in the mouse embryo and placenta: possible role in patterning of the extra-embryonic membranes.
Volume: 204
Issue: 3
Pages: 219-27
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Publication
9560346 | J:47384
First Author: Halenbeck R
Year: 1998
Journal: Curr Biol
Title: CPAN, a human nuclease regulated by the caspase-sensitive inhibitor DFF45.
Volume: 8
Issue: 9
Pages: 537-40
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Publication
9689044 | J:49086
First Author: Mukae N
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: Molecular cloning and characterization of human caspase-activated DNase.
Volume: 95
Issue: 16
Pages: 9123-8
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Publication
11959977 | J:76075
First Author: Dames SA
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.
Volume: 99
Issue: 8
Pages: 5271-6
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Publication
12421990 | J:80068
First Author: Quintana FJ
Year: 2002
Journal: J Immunol
Title: DNA vaccination with heat shock protein 60 inhibits cyclophosphamide-accelerated diabetes.
Volume: 169
Issue: 10
Pages: 6030-5
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Publication
16085056 | J:100948
First Author: Bae SY
Year: 2005
Journal: Biochim Biophys Acta
Title: Y+ and y+ L arginine transporters in neuronal cells expressing tyrosine hydroxylase.
Volume: 1745
Issue: 1
Pages: 65-73
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Publication
16204257 | J:104102
First Author: Lechardeur D
Year: 2005
Journal: J Biol Chem
Title: Oligomerization state of the DNA fragmentation factor in normal and apoptotic cells.
Volume: 280
Issue: 48
Pages: 40216-25
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Publication
16884849 | J:114446
First Author: Dandoy-Dron F
Year: 2006
Journal: Neurosci Lett
Title: Infection by ME7 prion is not modified in transgenic mice expressing the yeast chaperone Hsp104 in neurons.
Volume: 405
Issue: 3
Pages: 181-5
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Publication
16973670 | J:119992
First Author: Rebuzzini P
Year: 2007
Journal: Carcinogenesis
Title: Inhibition of gene amplification in telomerase deficient immortalized mouse embryonic fibroblasts.
Volume: 28
Issue: 3
Pages: 553-9
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Publication
16962992 | J:119993
First Author: Huang R
Year: 2006
Journal: Arch Biochem Biophys
Title: Direct interaction between caldesmon and cortactin.
Volume: 456
Issue: 2
Pages: 175-82
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Publication
19564421 | J:152611
First Author: Shin MH
Year: 2009
Journal: Mol Cell Biol
Title: Time-dependent activation of Phox2a by the cyclic AMP pathway modulates onset and duration of p27Kip1 transcription.
Volume: 29
Issue: 18
Pages: 4878-90
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Publication
18318786 | J:134451
First Author: Wang L
Year: 2008
Journal: Ann Hum Genet
Title: Polymorphisms of the tumor suppressor gene LSAMP are associated with left main coronary artery disease.
Volume: 72
Issue: Pt 4
Pages: 443-53
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Publication
23078884 | J:203896
First Author: Liu ZJ
Year: 2012
Journal: Atherosclerosis
Title: Notch activation induces endothelial cell senescence and pro-inflammatory response: implication of Notch signaling in atherosclerosis.
Volume: 225
Issue: 2
Pages: 296-303
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Publication
25633318 | J:241341
First Author: Jiang H
Year: 2015
Journal: Arterioscler Thromb Vasc Biol
Title: Tyrosine kinase receptor B protects against coronary artery disease and promotes adult vasculature integrity by regulating Ets1-mediated VE-cadherin expression.
Volume: 35
Issue: 3
Pages: 580-8
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Publication
31539914 | J:289467
First Author: Xu S
Year: 2019
Journal: Eur Heart J
Title: The novel coronary artery disease risk gene JCAD/KIAA1462 promotes endothelial dysfunction and atherosclerosis.
Volume: 40
Issue: 29
Pages: 2398-2408
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Publication
34307380 | J:340205
 
First Author: Kai H
Year: 2021
Journal: Front Cell Dev Biol
Title: LncRNA NORAD Promotes Vascular Endothelial Cell Injury and Atherosclerosis Through Suppressing VEGF Gene Transcription via Enhancing H3K9 Deacetylation by Recruiting HDAC6.
Volume: 9
Pages: 701628
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Publication
35062066 | J:319770
 
First Author: Hueso M
Year: 2022
Journal: Biomed Pharmacother
Title: MiR-125b downregulates macrophage scavenger receptor type B1 and reverse cholesterol transport.
Volume: 146
Pages: 112596
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Publication
34965503 | J:319772
 
First Author: Sandrini L
Year: 2022
Journal: Biomed Pharmacother
Title: The α2-adrenergic receptor pathway modulating depression influences the risk of arterial thrombosis associated with BDNFVal66Met polymorphism.
Volume: 146
Pages: 112557
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Protein
Q8C535
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
Q7TS81
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
Q8CA98
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
A0A1W2P7L3
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
Q8BP66
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein Domain
IPR006130 | Asp/Orn_carbamoylTrfase
Type: Family
Description: This family contains two related enzymes:Aspartate carbamoyltransferase () (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novobiosynthesis of pyrimidine nucleotides []. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyrB) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi-functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals []) that also catalyses other steps of the biosynthesis of pyrimidines.Ornithine carbamoyltransferase () (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals, this enzyme participates in the urea cycle []and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine [](the arginine deaminase pathway).It has been shown []that these two enzymes are evolutionary related. The predicted secondary structure of both enzymes are similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies [], to be implicated in binding the phosphoryl group of carbamoyl phosphate.
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Protein Domain
IPR004721 | DHOdimr
Type: Family
Description: Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ), where it is classified as a non-peptidase homologue. DHOase catalyses the third step in the de novobiosynthesis of pyrimidine, the conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. Dihydroorotase binds a zinc ion which is required for its catalytic activity [].In bacteria, DHOase is a dimer of identical chains of about 400 amino-acid residues (gene pyrC). In the metazoa, DHOase is part of a large multi-functional protein known as 'rudimentary' in Drosophila melanogaster and CAD in mammals and which catalyzes the first three steps of pyrimidine biosynthesis []. The DHOase domain is located in the central part of this polyprotein. In yeast, DHOase is encoded by a monofunctional protein (gene URA4). However, a defective DHOase domain []is found in a multifunctional protein (gene URA2) that catalyzes the first two steps of pyrimidine biosynthesis.The comparison of DHOase sequences from various sources shows []that there are two highly conserved regions. The first located in the N-terminal extremity contains two histidine residues suggested []to be involved in binding the zinc ion. The second is found in the C-terminal part. Members of this family of proteins are predicted to adopt a TIM barrel fold [].This family represents the homodimeric form of dihydroorotase . It is found in bacteria, plants and fungi; URA4 of yeast is a member of this group of sequences.
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Protein Domain
IPR036901 | Asp/Orn_carbamoylTrfase_sf
Type: Homologous_superfamily
Description: This domain superfamily contains two related enzymes:Aspartate carbamoyltransferase () (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novobiosynthesis of pyrimidine nucleotides []. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyrB) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi-functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals []) that also catalyses other steps of the biosynthesis ofpyrimidines.Ornithine carbamoyltransferase () (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle []and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine [](the arginine deaminase pathway).It has been shown []that these two enzymes are evolutionary related. The predicted secondary structure of both enzymes are similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies [], to be implicated in binding the phosphoryl group of carbamoyl phosphate.
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Publication
24925974 | J:227099
First Author: Shang MM
Year: 2014
Journal: Arterioscler Thromb Vasc Biol
Title: Lim domain binding 2: a key driver of transendothelial migration of leukocytes and atherosclerosis.
Volume: 34
Issue: 9
Pages: 2068-77
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Publication
16254213 | J:117515
First Author: Walter DH
Year: 2005
Journal: Circ Res
Title: Impaired CXCR4 signaling contributes to the reduced neovascularization capacity of endothelial progenitor cells from patients with coronary artery disease.
Volume: 97
Issue: 11
Pages: 1142-51
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Publication
23275384 | J:210277
First Author: Kränkel N
Year: 2013
Journal: Circulation
Title: Novel insights into the critical role of bradykinin and the kinin B2 receptor for vascular recruitment of circulating endothelial repair-promoting mononuclear cell subsets: alterations in patients with coronary disease.
Volume: 127
Issue: 5
Pages: 594-603
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Publication
34957248 | J:319369
 
First Author: Li B
Year: 2021
Journal: Front Cardiovasc Med
Title: The Association and Pathogenesis of SERPINA3 in Coronary Artery Disease.
Volume: 8
Pages: 756889
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Publication
36532779 | J:338951
 
First Author: Horckmans M
Year: 2022
Journal: Front Pharmacol
Title: Loss-of-function N178T variant of the human P2Y(4) receptor is associated with decreased severity of coronary artery disease and improved glucose homeostasis.
Volume: 13
Pages: 1049696
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Publication
27513923 | J:237247
First Author: Lu Q
Year: 2016
Journal: PLoS Biol
Title: Angiogenic Factor AGGF1 Activates Autophagy with an Essential Role in Therapeutic Angiogenesis for Heart Disease.
Volume: 14
Issue: 8
Pages: e1002529
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Publication
26020946 | J:224773
First Author: Nurnberg ST
Year: 2015
Journal: PLoS Genet
Title: Coronary Artery Disease Associated Transcription Factor TCF21 Regulates Smooth Muscle Precursor Cells That Contribute to the Fibrous Cap.
Volume: 11
Issue: 5
Pages: e1005155
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Publication
35653516 | J:335230
First Author: Wood A
Year: 2023
Journal: Cardiovasc Res
Title: PHACTR1 modulates vascular compliance but not endothelial function: a translational study.
Volume: 119
Issue: 2
Pages: 599-610
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Publication
34176299 | J:309184
First Author: Mizoguchi T
Year: 2021
Journal: Circ Res
Title: Coronary Disease Association With ADAMTS7 Is Due to Protease Activity.
Volume: 129
Issue: 4
Pages: 458-470
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Publication
22479590 | J:240263
First Author: Herrera-Molina R
Year: 2012
Journal: PLoS One
Title: Astrocytic αVβ3 integrin inhibits neurite outgrowth and promotes retraction of neuronal processes by clustering Thy-1.
Volume: 7
Issue: 3
Pages: e34295
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Publication
7805242 | J:37907
First Author: Hirozane T
Year: 1995
Journal: Circulation
Title: Experimental graft coronary artery disease in a murine heterotopic cardiac transplant model.
Volume: 91
Issue: 2
Pages: 386-92
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Publication
23152889 | J:195469
First Author: Tobón KE
Year: 2012
Journal: PLoS One
Title: MicroRNA 142-3p mediates post-transcriptional regulation of D1 dopamine receptor expression.
Volume: 7
Issue: 11
Pages: e49288
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Publication
26966275 | J:250372
First Author: Zhao Y
Year: 2016
Journal: Arterioscler Thromb Vasc Biol
Title: Network-Based Identification and Prioritization of Key Regulators of Coronary Artery Disease Loci.
Volume: 36
Issue: 5
Pages: 928-41
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Publication
28385496 | J:281512
First Author: Stitziel NO
Year: 2017
Journal: J Am Coll Cardiol
Title: ANGPTL3 Deficiency and Protection Against Coronary Artery Disease.
Volume: 69
Issue: 16
Pages: 2054-2063
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Publication
35690006 | J:345339
 
First Author: Luo T
Year: 2022
Journal: J Mol Cell Cardiol
Title: Deficiency of proline/serine-rich coiled-coil protein 1 (PSRC1) accelerates trimethylamine N-oxide-induced atherosclerosis in ApoE(-/-) mice.
Volume: 170
Pages: 60-74
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Publication
36932468 | J:345389
First Author: Pan H
Year: 2023
Journal: Clin Transl Med
Title: Proline/serine-rich coiled-coil protein 1 inhibits macrophage inflammation and delays atherosclerotic progression by binding to Annexin A2.
Volume: 13
Issue: 3
Pages: e1220
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Protein
O88862
Organism: Mus musculus/domesticus
Length: 35  
Fragment?: true
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Publication
8163532 | -
First Author: Hayashi S
Year: 1994
Journal: J Biol Chem
Title: Amphibian allantoinase. Molecular cloning, tissue distribution, and functional expression.
Volume: 269
Issue: 16
Pages: 12269-76
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Publication
1803816 | -
First Author: Buckholz RG
Year: 1991
Journal: Yeast
Title: The allantoinase (DAL1) gene of Saccharomyces cerevisiae.
Volume: 7
Issue: 9
Pages: 913-23
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Publication
15278241 | -
First Author: Brichta DM
Year: 2004
Journal: Arch Microbiol
Title: Pseudomonas aeruginosa dihydroorotases: a tale of three pyrCs.
Volume: 182
Issue: 1
Pages: 7-17
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Protein Domain
IPR004722 | DHOase
Type: Family
Description: Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ), and includes peptides classified as a non-peptidase homologues. DHOase catalyses the third step in the de novobiosynthesis of pyrimidine, the conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. Dihydroorotase binds a zinc ion which is required for its catalytic activity [].In bacteria, DHOase is a dimer of identical chains of about 400 amino-acid residues (gene pyrC). In higher eukaryotes, DHOase is part of a large multi-functional protein known as 'rudimentary' in Drosophila melanogaster and CAD in mammals and which catalyzes the first three steps of pyrimidine biosynthesis []. The DHOase domain is located in the central part of this polyprotein. In yeasts, DHOase is encoded by a monofunctional protein (gene URA4). However, a defective DHOase domain []is found in a multifunctional protein (gene URA2) that catalyzes the first two steps of pyrimidine biosynthesis.The comparison of DHOase sequences from various sources shows []that there are two highly conserved regions. The first located in the N-terminal extremity contains two histidine residues suggested []to be involved in binding the zinc ion. The second is found in the C-terminal part. Members of this family of proteins are predicted to adopt a TIM barrel fold [].Dihydroorotase 'multifunctional complex type' , in contrast to the homodimeric type of dihydroorotase found in Escherichia coli, tends to appear in a large multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and Pseudomonas aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present.
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Protein Domain
IPR002195 | Dihydroorotase_CS
Type: Conserved_site
Description: This group contains a number of protein families, example are:Archaeal and bacterial dihydroorotase () (DHOase)Allantoinase ()Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ), where it is classified as a non-peptidase homologue. DHOase catalyses the third step in the de novobiosynthesis of pyrimidine, the conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. Dihydroorotase binds a zinc ion which is required for its catalytic activity [].In bacteria, DHOase is a dimer of identical chains of about 400 amino-acid residues (gene pyrC) []. In higher eukaryotes, DHOase is part of a large multi-functional protein known as 'rudimentary' in Drosophila melanogaster and CAD in mammals and which catalyzes the first three steps of pyrimidine biosynthesis []. The DHOase domain is located in the central part of this polyprotein. In yeasts, DHOase is encoded by a monofunctional protein (gene URA4). However, a defective DHOase domain []is found in a multifunctional protein (gene URA2) that catalyzes the first two steps of pyrimidine biosynthesis.The comparison of DHOase sequences from various sources shows []that there are two highly conserved regions. The first located in the N-terminal extremity contains two histidine residues suggested []to be involved in binding the zinc ion. The second is found in the C-terminal part. Members of this family of proteins are predicted to adopt a TIM barrel fold [].Allantoinase () is the enzyme that hydrolyzes allantoin into allantoate. In yeast (gene DAL1) [], it is the first enzyme in the allantoin degradation pathway; in amphibians []and fishs it catalyzes the second step in the degradation of uric acid. The sequence of allantoinase is evolutionary related to that of DHOases.
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Publication
1671037 | -
First Author: Brown DC
Year: 1991
Journal: J Biol Chem
Title: Dihydroorotase from Escherichia coli. Substitution of Co(II) for the active site Zn(II).
Volume: 266
Issue: 3
Pages: 1597-604
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Publication
2897615 | -
First Author: Guyonvarch A
Year: 1988
Journal: Mol Gen Genet
Title: Structure of the Saccharomyces cerevisiae URA4 gene encoding dihydroorotase.
Volume: 212
Issue: 1
Pages: 134-41
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Publication
8098212 | -
First Author: Davidson JN
Year: 1993
Journal: Bioessays
Title: The evolutionary history of the first three enzymes in pyrimidine biosynthesis.
Volume: 15
Issue: 3
Pages: 157-64
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Publication
33123157 | J:337285
 
First Author: Chernomordik F
Year: 2020
Journal: Front Immunol
Title: The Role of T Cells Reactive to the Cathelicidin Antimicrobial Peptide LL-37 in Acute Coronary Syndrome and Plaque Calcification.
Volume: 11
Pages: 575577
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Publication
2570735 | -
First Author: Souciet JL
Year: 1989
Journal: Gene
Title: Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex.
Volume: 79
Issue: 1
Pages: 59-70
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Protein Domain
IPR005483 | CbamoylP_synth_lsu_CPSase_dom
Type: Domain
Description: Carbamoyl phosphate synthase (CPSase) is a heterodimeric enzyme composed of a small and a large subunit (with the exception of CPSase III, see below). CPSase catalyses the synthesis of carbamoyl phosphate from biocarbonate, ATP and glutamine () or ammonia (), and represents the first committed step in pyrimidine and arginine biosynthesis in prokaryotes and eukaryotes, and in the urea cycle in most terrestrial vertebrates [, ]. CPSase has three active sites, one in the small subunit and two in the large subunit. The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia. The large subunit has two homologous carboxy phosphate domains, both of which have ATP-binding sites; however, the N-terminal carboxy phosphate domain catalyses the phosphorylation of biocarbonate, while the C-terminal domain catalyses the phosphorylation of the carbamate intermediate []. The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase () (ACC), propionyl-CoA carboxylase () (PCCase), pyruvate carboxylase () (PC) and urea carboxylase ().Most prokaryotes carry one form of CPSase that participates in both arginine and pyrimidine biosynthesis, however certain bacteria can have separate forms. The large subunit in bacterial CPSase has four structural domains: the carboxy phosphate domain 1, the oligomerisation domain, the carbamoyl phosphate domain 2 and the allosteric domain []. CPSase heterodimers from Escherichia coli contain two molecular tunnels: an ammonia tunnel and a carbamate tunnel. These inter-domain tunnels connect the three distinct active sites, and function as conduits for the transport of unstable reaction intermediates (ammonia and carbamate) between successive active sites []. The catalytic mechanism of CPSase involves the diffusion of carbamate through the interior of the enzyme from the site of synthesis within the N-terminal domain of the large subunit to the site of phosphorylation within the C-terminal domain.Eukaryotes have two distinct forms of CPSase: a mitochondrial enzyme (CPSase I) that participates in both arginine biosynthesis and the urea cycle; and a cytosolic enzyme (CPSase II) involved in pyrimidine biosynthesis. CPSase II occurs as part of a multi-enzyme complex along with aspartate transcarbamoylase and dihydroorotase; this complex is referred to as the CAD protein []. The hepatic expression of CPSase is transcriptionally regulated by glucocorticoids and/or cAMP []. There is a third form of the enzyme, CPSase III, found in fish, which uses glutamine as a nitrogen source instead of ammonia []. CPSase III is closely related to CPSase I, and is composed of a single polypeptide that may have arisen from gene fusion of the glutaminase and synthetase domains []. This entry represents the CPSase domain of the large subunit of carbamoyl phosphate synthase.
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Protein Domain
IPR006275 | CarbamoylP_synth_lsu
Type: Family
Description: Carbamoyl phosphate synthase (CPSase) is a heterodimeric enzyme composed of a small and a large subunit (with the exception of CPSase III, see below). CPSase catalyses the synthesis of carbamoyl phosphate from biocarbonate, ATP and glutamine () or ammonia (), and represents the first committed step in pyrimidine and arginine biosynthesis in prokaryotes and eukaryotes, and in the urea cycle in most terrestrial vertebrates [, ]. CPSase has three active sites, one in the small subunit and two in the large subunit. The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia. The large subunit has two homologous carboxy phosphate domains, both of which have ATP-binding sites; however, the N-terminal carboxy phosphate domain catalyses the phosphorylation of biocarbonate, while the C-terminal domain catalyses the phosphorylation of the carbamate intermediate []. The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase () (ACC), propionyl-CoA carboxylase () (PCCase), pyruvate carboxylase () (PC) and urea carboxylase ().Most prokaryotes carry one form of CPSase that participates in both arginine and pyrimidine biosynthesis, however certain bacteria can have separate forms. The large subunit in bacterial CPSase has four structural domains: the carboxy phosphate domain 1, the oligomerisation domain, the carbamoyl phosphate domain 2 and the allosteric domain []. CPSase heterodimers from Escherichia coli contain two molecular tunnels: an ammonia tunnel and a carbamate tunnel. These inter-domain tunnels connect the three distinct active sites, and function as conduits for the transport of unstable reaction intermediates (ammonia and carbamate) between successive active sites []. The catalytic mechanism of CPSase involves the diffusion of carbamate through the interior of the enzyme from the site of synthesis within the N-terminal domain of the large subunit to the site of phosphorylation within the C-terminal domain.Eukaryotes have two distinct forms of CPSase: a mitochondrial enzyme (CPSase I) that participates in both arginine biosynthesis and the urea cycle; and a cytosolic enzyme (CPSase II) involved in pyrimidine biosynthesis. CPSase II occurs as part of a multi-enzyme complex along with aspartate transcarbamoylase and dihydroorotase; this complex is referred to as the CAD protein []. The hepatic expression of CPSase is transcriptionally regulated by glucocorticoids and/or cAMP []. There is a third form of the enzyme, CPSase III, found in fish, which uses glutamine as a nitrogen source instead of ammonia []. CPSase III is closely related to CPSase I, and is composed of a single polypeptide that may have arisen from gene fusion of the glutaminase and synthetase domains []. This entry represents glutamine-dependent CPSase () from prokaryotes and eukaryotes (CPSase II).
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Protein
P11725
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
Q8R1A8
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
Q9CWQ9
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
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Protein
Q543H3
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Publication
3015959 | -
First Author: Lerner CG
Year: 1986
Journal: J Biol Chem
Title: Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).
Volume: 261
Issue: 24
Pages: 11156-65
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Publication
2662961 | -
First Author: Takiguchi M
Year: 1989
Journal: Bioessays
Title: Evolutionary aspects of urea cycle enzyme genes.
Volume: 10
Issue: 5
Pages: 163-6
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Publication
6377306 | -
First Author: Ke HM
Year: 1984
Journal: Proc Natl Acad Sci U S A
Title: Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.
Volume: 81
Issue: 13
Pages: 4037-40
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Publication
6379651 | -
First Author: Houghton JE
Year: 1984
Journal: Proc Natl Acad Sci U S A
Title: Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12.
Volume: 81
Issue: 15
Pages: 4864-8
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Publication
10089390 | -
First Author: Thoden JB
Year: 1999
Journal: Acta Crystallogr D Biol Crystallogr
Title: The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution.
Volume: 55
Issue: Pt 1
Pages: 8-24
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Publication
17397987 | -
First Author: Schoneveld OJ
Year: 2007
Journal: Biochimie
Title: cyclicAMP and glucocorticoid responsiveness of the rat carbamoylphosphate synthetase gene requires the interplay of upstream regulatory units.
Volume: 89
Issue: 5
Pages: 574-80
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Publication
8916922 | -
First Author: Stapleton MA
Year: 1996
Journal: Biochemistry
Title: Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase.
Volume: 35
Issue: 45
Pages: 14352-61
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Publication
12379099 | -
First Author: Kim J
Year: 2002
Journal: Biochemistry
Title: Structural defects within the carbamate tunnel of carbamoyl phosphate synthetase.
Volume: 41
Issue: 42
Pages: 12575-81
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Publication
17451989 | -
First Author: Saha N
Year: 2007
Journal: Comp Biochem Physiol B Biochem Mol Biol
Title: Air-breathing catfish, Clarias batrachus upregulates glutamine synthetase and carbamyl phosphate synthetase III during exposure to high external ammonia.
Volume: 147
Issue: 3
Pages: 520-30
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Publication
7932737 | -
First Author: Hong J
Year: 1994
Journal: J Mol Biol
Title: Carbamyl phosphate synthetase III, an evolutionary intermediate in the transition between glutamine-dependent and ammonia-dependent carbamyl phosphate synthetases.
Volume: 243
Issue: 1
Pages: 131-40
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Publication
2982857 | -
First Author: Zalkin H
Year: 1985
Journal: J Biol Chem
Title: Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
Volume: 260
Issue: 6
Pages: 3350-4
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Protein Domain
IPR017926 | GATASE
Type: Domain
Description: Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group []. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified [, ]: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). Class-I (or type 1) GATase domains have been found in the following enzymes:The second component of anthranilate synthase (AS) []. AS catalyzes the biosynthesis of anthranilate from chorismate and glutamine. AS is generally a dimeric enzyme: the first component can synthesize anthranilate using ammonia rather than glutamine, whereas component II provides the GATase activity []. In some bacteria and in fungi the GATase component of AS is part of a multifunctional protein that also catalyzes other steps of the biosynthesis of tryptophan.The second component of 4-amino-4-deoxychorismate (ADC) synthase, a dimeric prokaryotic enzyme that functions in the pathway that catalyzes the biosynthesis of para-aminobenzoate (PABA) from chorismate and glutamine. The second component (gene pabA) provides the GATase activity [].CTP synthase. CTP synthase catalyzes the final reaction in the biosynthesis of pyrimidine, the ATP-dependent formation of CTP from UTP and glutamine. CTP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the C-terminal section [].GMP synthase (glutamine-hydrolyzing). GMP synthase catalyzes the ATP-dependent formation of GMP from xanthosine 5'-phosphate and glutamine. GMP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the N-terminal section [, ].Glutamine-dependent carbamoyl-phosphate synthase (GD-CPSase); an enzyme involved in both arginine and pyrimidine biosynthesis and which catalyzes the ATP-dependent formation of carbamoyl phosphate from glutamine and carbon dioxide. In bacteria GD-CPSase is composed of two subunits: the large chain (gene carB) provides the CPSase activity, while the small chain (gene carA) provides the GATase activity. In yeast the enzyme involved in arginine biosynthesis is also composed of two subunits: CPA1 (GATase), and CPA2 (CPSase). In most eukaryotes, the first three steps of pyrimidine biosynthesis are catalyzed by a large multifunctional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals). The GATase domain is located at the N-terminal extremity of this polyprotein [].Phosphoribosylformylglycinamidine synthase, an enzyme that catalyzes the fourth step in the de novo biosynthesis of purines. In some species of bacteria and rchaea, FGAM synthase II is composed of two subunits: a small chain (gene purQ) which provides the GATase activity and a large chain (gene purL) which provides the aminator activity. In eukaryotes and Gram-negative bacteria a single polypeptide (large type of purL) contains a FGAM synthethase domain and the GATase as the C-terminal domain [].Imidazole glycerol phosphate synthase subunit hisH, an enzyme that catalyzes the fifth step in the biosynthesis of histidine.A triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity [, ]. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.
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Protein Domain
IPR005479 | CbamoylP_synth_lsu-like_ATP-bd
Type: Domain
Description: Carbamoyl phosphate synthase (CPSase) is a heterodimeric enzyme composed of a small and a large subunit (with the exception of CPSase III, see below). CPSase catalyses the synthesis of carbamoyl phosphate from biocarbonate, ATP and glutamine () or ammonia (), and represents the first committed step in pyrimidine and arginine biosynthesis in prokaryotes and eukaryotes, and in the urea cycle in most terrestrial vertebrates [, ]. CPSase has three active sites, one in the small subunit and two in the large subunit. The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia. The large subunit has two homologous carboxy phosphate domains, both of which have ATP-binding sites; however, the N-terminal carboxy phosphate domain catalyses the phosphorylation of biocarbonate, while the C-terminal domain catalyses the phosphorylation of the carbamate intermediate []. The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase () (ACC), propionyl-CoA carboxylase () (PCCase), pyruvate carboxylase () (PC) and urea carboxylase ().Most prokaryotes carry one form of CPSase that participates in both arginine and pyrimidine biosynthesis, however certain bacteria can have separate forms. The large subunit in bacterial CPSase has four structural domains: the carboxy phosphate domain 1, the oligomerisation domain, the carbamoyl phosphate domain 2 and the allosteric domain []. CPSase heterodimers from Escherichia coli contain two molecular tunnels: an ammonia tunnel and a carbamate tunnel. These inter-domain tunnels connect the three distinct active sites, and function as conduits for the transport of unstable reaction intermediates (ammonia and carbamate) between successive active sites []. The catalytic mechanism of CPSase involves the diffusion of carbamate through the interior of the enzyme from the site of synthesis within the N-terminal domain of the large subunit to the site of phosphorylation within the C-terminal domain.Eukaryotes have two distinct forms of CPSase: a mitochondrial enzyme (CPSase I) that participates in both arginine biosynthesis and the urea cycle; and a cytosolic enzyme (CPSase II) involved in pyrimidine biosynthesis. CPSase II occurs as part of a multi-enzyme complex along with aspartate transcarbamoylase and dihydroorotase; this complex is referred to as the CAD protein []. The hepatic expression of CPSase is transcriptionally regulated by glucocorticoids and/or cAMP []. There is a third form of the enzyme, CPSase III, found in fish, which uses glutamine as a nitrogen source instead of ammonia []. CPSase III is closely related to CPSase I, and is composed of a single polypeptide that may have arisen from gene fusion of the glutaminase and synthetase domains []. This entry represents the ATP-binding domain found in the large subunit of carbamoyl phosphate synthase, as well as in other proteins, including acetyl-CoA carboxylases and pyruvate carboxylases.
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Protein
Q561M8
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: true
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Publication
3109911 | -
First Author: Baur H
Year: 1987
Journal: Eur J Biochem
Title: Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli.
Volume: 166
Issue: 1
Pages: 111-7
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Publication
9144792 | -
First Author: Holm L
Year: 1997
Journal: Proteins
Title: An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.
Volume: 28
Issue: 1
Pages: 72-82
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Publication
10387030 | -
First Author: Raushel FM
Year: 1999
Journal: Biochemistry
Title: The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia.
Volume: 38
Issue: 25
Pages: 7891-9
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Publication
11212301 | -
First Author: Holden HM
Year: 1999
Journal: Cell Mol Life Sci
Title: Carbamoyl phosphate synthetase: an amazing biochemical odyssey from substrate to product.
Volume: 56
Issue: 5-6
Pages: 507-22
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Publication
- | J:29622
 
First Author: Guenet JL
Year: 1978
Journal: Mouse News Lett
Title: Mutant Stocks: Alphabetical list of named mutant genes (except T locus alleles)
Volume: 59
Pages: 50-54
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Protein
Q8C196
Organism: Mus musculus/domesticus
Length: 1500  
Fragment?: false
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Protein
H3BL62
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: true
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Protein
A0A0G2JF64
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
D3YZC0
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
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Protein
A2AEQ5
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
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Protein
Q3THK7
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: false
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Protein
P70698
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
P70303
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
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Protein
A0A0G2JFQ5
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein
Q3TVD9
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
B2RRH9
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: false
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Publication
10449718 | -
First Author: Knöchel T
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Volume: 96
Issue: 17
Pages: 9479-84
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Publication
15301531 | -
First Author: Anand R
Year: 2004
Journal: Biochemistry
Title: Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.
Volume: 43
Issue: 32
Pages: 10328-42
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Publication
28956599 | -
First Author: Reddick JJ
Year: 2017
Journal: Biochemistry
Title: First Biochemical Characterization of a Methylcitric Acid Cycle from Bacillus subtilis Strain 168.
Volume: 56
Issue: 42
Pages: 5698-5711
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Protein
Q91ZA3
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
Q99MR8
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q3UGC8
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
Q62043
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: true
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Publication
8548458 | -
First Author: Tesmer JJ
Year: 1996
Journal: Nat Struct Biol
Title: The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Volume: 3
Issue: 1
Pages: 74-86
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Publication
2679363 | -
 
First Author: Crawford IP
Year: 1989
Journal: Annu Rev Microbiol
Title: Evolution of a biosynthetic pathway: the tryptophan paradigm.
Volume: 43
Pages: 567-600
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Publication
3298209 | -
First Author: Weng ML
Year: 1987
Journal: J Bacteriol
Title: Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain.
Volume: 169
Issue: 7
Pages: 3023-8
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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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