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Your query returned 29 entries. Printable version
EC | 1.4.1.13 | ||||||||||||||||
Accepted name: | glutamate synthase (NADPH) | ||||||||||||||||
Reaction: | 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ (overall reaction) (1a) L-glutamate + NH3 = L-glutamine + H2O (1b) L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+ |
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Other name(s): | glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT | ||||||||||||||||
Systematic name: | L-glutamate:NADP+ oxidoreductase (transaminating) | ||||||||||||||||
Comments: | Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, α and β. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons from the cosubstrate. The NH3 is channeled within the α subunit through a 31 Å channel. The chanelling is very efficient and in the intact α-β complex ammonia is produced only within the complex. In the absence of the β subunit, coupling between the two domains of the α subunit is compromised and some ammonium can leak. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37213-53-9 | ||||||||||||||||
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EC | 1.4.1.14 | ||||||||||||||||
Accepted name: | glutamate synthase (NADH) | ||||||||||||||||
Reaction: | 2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+ (1a) L-glutamate + NH3 = L-glutamine + H2O (1b) L-glutamate + NAD+ + H2O = NH3 + 2-oxoglutarate + NADH + H+ |
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Other name(s): | glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase | ||||||||||||||||
Systematic name: | L-glutamate:NAD+ oxidoreductase (transaminating) | ||||||||||||||||
Comments: | A flavoprotein (FMN). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2, glutamate dehydrogenase). | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65589-88-0 | ||||||||||||||||
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EC | 1.4.7.1 | ||||||||||||||||
Accepted name: | glutamate synthase (ferredoxin) | ||||||||||||||||
Reaction: | 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ (overall reaction) (1a) L-glutamate + NH3 = L-glutamine + H2O (1b) L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ |
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Other name(s): | ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent) | ||||||||||||||||
Systematic name: | L-glutamate:ferredoxin oxidoreductase (transaminating) | ||||||||||||||||
Comments: | Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6]. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-56-3 | ||||||||||||||||
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EC | 2.6.1.97 | ||||||||||||||||
Accepted name: | archaeosine synthase | ||||||||||||||||
Reaction: | L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O = L-glutamate + archaeine15 in tRNA | ||||||||||||||||
Glossary: | 7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine archaeine = 7-deaza-7-carbamidoylguanine = base G* archaeosine = G* = 7-amidino-7-deazaguanosine |
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Other name(s): | ArcS; TgtA2; MJ1022 (gene name); glutamine:preQ0-tRNA amidinotransferase (incorrect) | ||||||||||||||||
Systematic name: | L-glutamine:7-cyano-7-carbaguanine aminotransferase | ||||||||||||||||
Comments: | In Euryarchaeota the reaction is catalysed by ArcS [1,2]. In Crenarchaeota, which do not have an ArcS homologue, the reaction is catalysed either by a homologue of EC 6.3.4.20, 7-cyano-7-deazaguanine synthase that includes a glutaminase domain (cf. EC 3.5.1.2), or by a homologue of EC 1.7.1.13, preQ1 synthase [2]. The enzyme from the Euryarchaeon Methanocaldococcus jannaschii can also use arginine and ammonium as amino donors. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
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EC | 2.6.1.123 | ||||||||||||||||
Accepted name: | 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming) | ||||||||||||||||
Reaction: | chorismate + 2 L-glutamine + H2O = 4-amino-4-deoxychorismate + 2 L-glutamate + NH3 (overall reaction) (1a) 2 L-glutamine + 2 H2O = 2 L-glutamate + 2 NH3 (1b) chorismate + NH3 = (2S)-2-amino-4-deoxychorismate + H2O (1c) (2S)-2-amino-4-deoxychorismate + NH3 = 4-amino-4-deoxychorismate + NH3 |
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Other name(s): | ADCS (ambiguous); ADC synthase (ambiguous); pabAB (gene names) | ||||||||||||||||
Systematic name: | chorismate:L-glutamine aminotransferase (2-amino-4-deoxychorismate-forming) | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA subunit acts successively on two molecules of L-glutamine, hydrolysing each to L-glutamate and ammonia (cf. EC 3.5.1.2, glutaminase). The ammonia molecules are channeled to the active site of PabB, which catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
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EC | 3.4.12.5 | ||||||||||||||||
Transferred entry: | now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase | ||||||||||||||||
EC | 3.4.17.7 | ||||||||||||||||
Transferred entry: | acylmuramoyl-alanine carboxypeptidase. Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase | ||||||||||||||||
EC | 3.4.19.10 | ||||||||||||||||
Transferred entry: | acylmuramoyl-Ala peptidase. Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase | ||||||||||||||||
EC | 3.5.1.2 | ||||||||||||||||
Accepted name: | glutaminase | ||||||||||||||||
Reaction: | L-glutamine + H2O = L-glutamate + NH3 | ||||||||||||||||
Other name(s): | glutaminase I; L-glutaminase; glutamine aminohydrolase | ||||||||||||||||
Systematic name: | L-glutamine amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-47-2 | ||||||||||||||||
References: |
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EC | 3.5.1.20 | ||||||||||||||||
Accepted name: | citrullinase | ||||||||||||||||
Reaction: | L-citrulline + H2O = L-ornithine + CO2 + NH3 | ||||||||||||||||
Other name(s): | citrulline ureidase; citrulline hydrolase; L-citrulline 5-N-carbamoyldihydrolase | ||||||||||||||||
Systematic name: | L-citrulline N5-carbamoyldihydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 59088-17-4 | ||||||||||||||||
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EC | 3.5.1.21 | ||||||||||||||||
Accepted name: | N-acetyl-β-alanine deacetylase | ||||||||||||||||
Reaction: | N-acetyl-β-alanine + H2O = acetate + β-alanine | ||||||||||||||||
Systematic name: | N-acetyl-β-alanine amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-04-6 | ||||||||||||||||
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EC | 3.5.1.22 | ||||||||||||||||
Accepted name: | pantothenase | ||||||||||||||||
Reaction: | (R)-pantothenate + H2O = (R)-pantoate + β-alanine | ||||||||||||||||
For diagram of pantothenate catabolism, click here | |||||||||||||||||
Other name(s): | pantothenate hydrolase; pantothenate amidohydrolase | ||||||||||||||||
Systematic name: | (R)-pantothenate amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9076-90-8 | ||||||||||||||||
References: |
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EC | 3.5.1.23 | ||||||||||||||||
Accepted name: | ceramidase | ||||||||||||||||
Reaction: | a ceramide + H2O = a carboxylate + sphingosine | ||||||||||||||||
Glossary: | a ceramide = an N-acylsphingosine | ||||||||||||||||
Other name(s): | acylsphingosine deacylase; glycosphingolipid ceramide deacylase | ||||||||||||||||
Systematic name: | N-acylsphingosine amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-06-8 | ||||||||||||||||
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EC | 3.5.1.24 | ||||||||||||||||
Accepted name: | choloylglycine hydrolase | ||||||||||||||||
Reaction: | glycocholate + H2O = cholate + glycine | ||||||||||||||||
For diagram of cholic acid conjugates biosynthesis, click here | |||||||||||||||||
Glossary: | glycocholate = N-(3α,7α,12α-trihydroxy-5β-cholan-24-oyl)glycine cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate |
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Other name(s): | glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase | ||||||||||||||||
Systematic name: | glycocholate amidohydrolase | ||||||||||||||||
Comments: | Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-07-9 | ||||||||||||||||
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EC | 3.5.1.25 | ||||||||||||||||
Accepted name: | N-acetylglucosamine-6-phosphate deacetylase | ||||||||||||||||
Reaction: | N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate | ||||||||||||||||
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here | |||||||||||||||||
Other name(s): | acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase | ||||||||||||||||
Systematic name: | N-acetyl-D-glucosamine-6-phosphate amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-50-3 | ||||||||||||||||
References: |
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EC | 3.5.1.26 | ||||||||||||||||
Accepted name: | N4-(β-N-acetylglucosaminyl)-L-asparaginase | ||||||||||||||||
Reaction: | N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-β-D-glucosaminylamine + L-aspartate | ||||||||||||||||
Other name(s): | aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase | ||||||||||||||||
Systematic name: | N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase | ||||||||||||||||
Comments: | Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase] | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-24-5 | ||||||||||||||||
References: |
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EC | 3.5.1.27 | ||||||||||||||||
Deleted entry: | N-formylmethionylaminoacyl-tRNA deformylase. The activity is covered by EC 3.5.1.88, peptide deformylase | ||||||||||||||||
EC | 3.5.1.28 | ||||||||||||||||
Accepted name: | N-acetylmuramoyl-L-alanine amidase | ||||||||||||||||
Reaction: | Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides | ||||||||||||||||
Glossary: | thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium | ||||||||||||||||
Other name(s): | acetylmuramyl-L-alanine amidase; N-acetylmuramyl-L-alanine amidase; N-acylmuramyl-L-alanine amidase; acetylmuramoyl-alanine amidase; N-acetylmuramic acid L-alanine amidase; acetylmuramyl-alanine amidase; N-acetylmuramylalanine amidase; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II | ||||||||||||||||
Systematic name: | peptidoglycan amidohydrolase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-25-6 | ||||||||||||||||
References: |
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EC | 3.5.1.29 | ||||||||||||||||
Accepted name: | 2-(acetamidomethylene)succinate hydrolase | ||||||||||||||||
Reaction: | 2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2 | ||||||||||||||||
Other name(s): | α-(N-acetylaminomethylene)succinic acid hydrolase | ||||||||||||||||
Systematic name: | 2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating) | ||||||||||||||||
Comments: | Involved in the degradation of pyridoxin in Pseudomonas. | ||||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-09-1 | ||||||||||||||||
References: |
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EC | 3.5.1.37 | ||||||||||||||||
Deleted entry: | 4-L-aspartylglycosylamine amidohydrolase. Identical with EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase | ||||||||||||||||
EC | 3.5.1.38 | ||||||||||||||||
Accepted name: | glutamin-(asparagin-)ase | ||||||||||||||||
Reaction: | (1) L-glutamine + H2O = L-glutamate + NH3 (2) L-asparagine + H2O = L-aspartate + NH3 |
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Other name(s): | glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase | ||||||||||||||||
Systematic name: | L-glutamine(L-asparagine) amidohydrolase | ||||||||||||||||
Comments: | The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39335-03-0 | ||||||||||||||||
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EC | 3.5.1.52 | ||||||||||||||||
Accepted name: | peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase | ||||||||||||||||
Reaction: | Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue | ||||||||||||||||
Other name(s): | glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F | ||||||||||||||||
Systematic name: | N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase | ||||||||||||||||
Comments: | Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83534-39-8 | ||||||||||||||||
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EC | 3.5.1.69 | ||||||||||||||||
Accepted name: | glycosphingolipid deacylase | ||||||||||||||||
Reaction: | Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives | ||||||||||||||||
Other name(s): | glycosphingolipid ceramide deacylase | ||||||||||||||||
Systematic name: | glycosphingolipid amidohydrolase | ||||||||||||||||
Comments: | Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-53-0 | ||||||||||||||||
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EC | 3.5.1.80 | ||||||||||||||||
Deleted entry: | N-acetylgalactosamine-6-phosphate deacetylase. Identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase | ||||||||||||||||
EC | 4.3.2.10 | ||||||||||||||||
Accepted name: | imidazole glycerol-phosphate synthase | ||||||||||||||||
Reaction: | 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate (overall reaction) (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + NH3 = 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O |
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For diagram of histidine biosynthesis (late stages), click here | |||||||||||||||||
Other name(s): | IGP synthase; hisFH (gene names); HIS7 (gene name) | ||||||||||||||||
Systematic name: | 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate-lyase (L-glutamine-hydrolysing; 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide-forming) | ||||||||||||||||
Comments: | The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 Å tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
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EC | 6.3.4.2 | ||||||||||||||||
Accepted name: | CTP synthase (glutamine hydrolysing) | ||||||||||||||||
Reaction: | ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate (overall reaction) (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) ATP + UTP + NH3 = ADP + phosphate + CTP |
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Other name(s): | UTP—ammonia ligase; cytidine triphosphate synthetase; uridine triphosphate aminase; cytidine 5′-triphosphate synthetase; CTPS (gene name); pyrG (gene name); CTP synthase; UTP:ammonia ligase (ADP-forming) | ||||||||||||||||
Systematic name: | UTP:L-glutamine amido-ligase (ADP-forming) | ||||||||||||||||
Comments: | The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP [4,5]. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution [3,6]. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-56-7 | ||||||||||||||||
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EC | 6.3.5.6 | ||||||||||||||||
Accepted name: | asparaginyl-tRNA synthase (glutamine-hydrolysing) | ||||||||||||||||
Reaction: | ATP + L-aspartyl-tRNAAsn + L-glutamine + H2O = ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) ATP + L-aspartyl-tRNAAsn = ADP + 4-phosphooxy-L-aspartyl-tRNAAsn (1c) 4-phosphooxy-L-aspartyl-tRNAAsn + NH3 = L-asparaginyl-tRNAAsn + phosphate |
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Other name(s): | Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming); GatCAB | ||||||||||||||||
Systematic name: | L-aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming) | ||||||||||||||||
Comments: | This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis. In the first step, a non-discriminating ligase (EC 6.1.1.23, aspartate—tRNAAsn ligase) mischarges tRNAAsn with aspartate, leading to the formation of aspartyl-tRNAAsn. The aspartyl-tRNAAsn is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNAAsn (aspartyl-tRNAAsp is not a substrate for this enzyme). A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 30 Å tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. Bacterial GatCAB complexes also has the activity of EC 6.3.5.7 (glutaminyl-tRNA synthase [glutamine-hydrolysing]). | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37211-76-0 | ||||||||||||||||
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EC | 6.3.5.7 | ||||||||||||||||
Accepted name: | glutaminyl-tRNA synthase (glutamine-hydrolysing) | ||||||||||||||||
Reaction: | ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate (overall reaction) (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) ATP + L-glutamyl-tRNAGln = ADP + 5-phosphooxy-L-glutamyl-tRNAGln (1c) 5-phosphooxy-L-glutamyl-tRNAGln + NH3 = L-glutaminyl-tRNAGln + phosphate |
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Other name(s): | Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming); GatCAB; GatFAB; GatDE | ||||||||||||||||
Systematic name: | L-glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming) | ||||||||||||||||
Comments: | In systems lacking discernible glutamine—tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate—tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this enzyme). A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 30 Å tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6 (asparaginyl-tRNA synthase [glutamine-hydrolysing]). | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52232-48-1 | ||||||||||||||||
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EC | 6.3.5.13 | ||||||||||||||||
Accepted name: | lipid II isoglutaminyl synthase (glutamine-hydrolysing) | ||||||||||||||||
Reaction: | ATP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol + L-glutamine + H2O = ADP + phosphate + β-D-GlcNAc-(1→4)-MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol + L-glutamate (overall reaction) (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) ATP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol = ADP + β-D-GlcNAc-(1→4)-MurNAc-L-Ala-γ-D-O-P-Glu-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol (1c) β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol + NH3 = β-D-GlcNAc-(1→4)-MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol + phosphate |
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Glossary: | lipid II = undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof | ||||||||||||||||
Other name(s): | MurT/GatD; MurT/GatD complex | ||||||||||||||||
Systematic name: | β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol:L-glutamine amidoligase (ADP-forming) | ||||||||||||||||
Comments: | The enzyme complex, found in Gram-positive bacteria, consists of two subunits. A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is channeled to a ligase subunit, which adds it to the activated D-glutamate residue of lipid II, converting it to an isoglutamine residue. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
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