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Your query returned 12 entries. Printable version
EC | 1.3.8.16 | ||||||||||||||
Accepted name: | 2-amino-4-deoxychorismate dehydrogenase | ||||||||||||||
Reaction: | (2S)-2-amino-4-deoxychorismate + FMN = 3-(1-carboxyvinyloxy)anthranilate + FMNH2 | ||||||||||||||
For diagram of enediyne antitumour antibiotic biosynthesis, click here | |||||||||||||||
Glossary: | (2S)-2-amino-4-deoxychorismate = (2S,3S)-3-(1-carboxyvinyloxy)-2,3-dihydroanthranilate 3-enolpyruvoylanthranilate = 3-(1-carboxyvinyloxy)anthranilate |
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Other name(s): | ADIC dehydrogenase; 2-amino-2-deoxyisochorismate dehydrogenase; SgcG | ||||||||||||||
Systematic name: | (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase | ||||||||||||||
Comments: | The sequential action of EC 2.6.1.86, 2-amino-4-deoxychorismate synthase and this enzyme leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 1.3.99.24 | ||||||||||||||
Transferred entry: | 2-amino-4-deoxychorismate dehydrogenase. Now EC 1.3.8.16, 2-amino-4-deoxychorismate dehydrogenase | ||||||||||||||
EC | 2.2.1.9 | ||||||||||||||
Accepted name: | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase | ||||||||||||||
Reaction: | isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2 | ||||||||||||||
Other name(s): | SEPHCHC synthase; MenD | ||||||||||||||
Systematic name: | isochorismate:2-oxoglutarate 4-oxopentanoatetransferase (decarboxylating) | ||||||||||||||
Comments: | Requires Mg2+ for maximal activity. This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1112282-73-1 | ||||||||||||||
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EC | 2.5.1.64 | ||||||||||||||
Transferred entry: | 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. The reaction that was attributed to this enzyme is now known to be catalysed by two separate enzymes: EC 2.2.1.9 (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase) and EC 4.2.99.20 (2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase) | ||||||||||||||
EC | 2.6.1.86 | ||||||||||||||
Accepted name: | 2-amino-4-deoxychorismate synthase | ||||||||||||||
Reaction: | (2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine | ||||||||||||||
For diagram of enediyne antitumour antibiotic biosynthesis, click here | |||||||||||||||
Glossary: | (2S)-2-amino-4-deoxychorismate = (2S,3S)-3-(1-carboxyvinyloxy)-2,3-dihydroanthranilate | ||||||||||||||
Other name(s): | ADIC synthase; 2-amino-2-deoxyisochorismate synthase; SgcD | ||||||||||||||
Systematic name: | (2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase | ||||||||||||||
Comments: | Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity [3,4]. | ||||||||||||||
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 | 3.3.2.1 | ||||||||||||||
Accepted name: | isochorismatase | ||||||||||||||
Reaction: | isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate | ||||||||||||||
For diagram of shikimate and chorismate biosynthesis, click here | |||||||||||||||
Glossary: | isochorismate = (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylate | ||||||||||||||
Other name(s): | 2,3-dihydro-2,3-dihydroxybenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoic synthase | ||||||||||||||
Systematic name: | isochorismate pyruvate-hydrolase | ||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of several siderophores, such as 2,3-dihydroxybenzoylglycine, enterobactin, bacillibactin, and vibriobactin. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-64-5 | ||||||||||||||
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EC | 4.1.3.27 | ||||||||||||||
Accepted name: | anthranilate synthase | ||||||||||||||
Reaction: | chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (overall reaction) (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) chorismate + NH3 = (2S)-2-amino-4-deoxychorismate + H2O (1c) (2S)-2-amino-4-deoxychorismate = anthranilate + pyruvate |
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For diagram of tryptophan biosynthesis, click here | |||||||||||||||
Other name(s): | anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpDE | ||||||||||||||
Systematic name: | chorismate pyruvate-lyase (amino-accepting; anthranilate-forming) | ||||||||||||||
Comments: | The enzyme, found in plants, fungi and bacteria is composed of two parts, a glutaminase subunit and a lyase subunit. The glutaminase produces ammonia that is channeled to the lyase subunit. In the absence of the glutaminase, the lyase can convert ammonia and chorismate into anthranilate. In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-59-8 | ||||||||||||||
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EC | 4.2.99.21 | ||||||||||||||
Accepted name: | isochorismate lyase | ||||||||||||||
Reaction: | isochorismate = salicylate + pyruvate | ||||||||||||||
Other name(s): | salicylate biosynthesis protein pchB; pyochelin biosynthetic protein PchB; isochorismate pyruvate lyase | ||||||||||||||
Systematic name: | isochorismate pyruvate-lyase (salicylate-forming) | ||||||||||||||
Comments: | This enzyme is part of the pathway of salicylate formation from chorismate, and forms an integral part of pathways that produce salicylate-derived siderophores, such as pyochelin and yersiniabactin. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
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EC | 5.4.4.2 | ||||||||||||||
Accepted name: | isochorismate synthase | ||||||||||||||
Reaction: | chorismate = isochorismate | ||||||||||||||
For diagram of shikimate and chorismate biosynthesis, click here | |||||||||||||||
Other name(s): | MenF | ||||||||||||||
Systematic name: | isochorismate hydroxymutase | ||||||||||||||
Comments: | Requires Mg2+. The reaction is reversible. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-53-9 | ||||||||||||||
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EC | 5.4.99.6 | ||||||||||||||
Transferred entry: | isochorismate synthase. Now EC 5.4.4.2, isochorismate synthase | ||||||||||||||
EC | 6.2.1.71 | ||||||||||||||
Accepted name: | 2,3-dihydroxybenzoate—[aryl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + 2,3-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 2,3-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction) (1a) ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate (1b) (2,3-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 2,3-dihydroxybenzoyl-[aryl-carrier protein] |
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Other name(s): | entE (gene name); vibE (gene name); dhbE (gene name); angE (gene name) | ||||||||||||||
Systematic name: | 2,3-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of 2,3-dihydroxybenzoate to (2,3-dihydroxybenzoyl)adenylate, followed by the transfer the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain of a specific non-ribosomal peptide synthase. For example, the EntE enzyme of Escherichia coli is part of the enterobactin synthase complex, the VibE enzyme of Vibrio cholerae is part of the vibriobactin synthase complex, and the DhbE enzyme of Bacillus subtilis is part of the bacillibactin synthase complex. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
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