The Enzyme Database

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EC 1.1.1.24     
Accepted name: quinate/shikimate dehydrogenase (NAD+)
Reaction: L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): quinate dehydrogenase (ambiguous); quinic dehydrogenase (ambiguous); quinate:NAD oxidoreductase; quinate 5-dehydrogenase (ambiguous); quinate:NAD+ 5-oxidoreductase
Systematic name: L-quinate:NAD+ 3-oxidoreductase
Comments: The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-28-8
References:
1.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693]
2.  Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483–491.
3.  Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem. Genet. 20 (1982) 271–286. [PMID: 7049157]
4.  Singh, S., Stavrinides, J., Christendat, D. and Guttman, D.S. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol. Biol. Evol. 25 (2008) 2221–2232. [DOI] [PMID: 18669580]
5.  Teramoto, H., Inui, M. and Yukawa, H. Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75 (2009) 3461–3468. [DOI] [PMID: 19376919]
6.  Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 97 (2013) 8139–8149. [DOI] [PMID: 23306642]
7.  Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Arch. Biochem. Biophys. 566 (2015) 85–99. [DOI] [PMID: 25524738]
[EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021]
 
 
EC 1.1.1.25     
Accepted name: shikimate dehydrogenase (NADP+)
Reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
For diagram of shikimate and chorismate biosynthesis, click here
Other name(s): shikimate dehydrogenase; dehydroshikimic reductase; shikimate oxidoreductase; shikimate:NADP+ oxidoreductase; 5-dehydroshikimate reductase; shikimate 5-dehydrogenase; 5-dehydroshikimic reductase; DHS reductase; shikimate:NADP+ 5-oxidoreductase; AroE
Systematic name: shikimate:NADP+ 3-oxidoreductase
Comments: NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-87-3
References:
1.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693]
2.  Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787–795. [PMID: 14367339]
3.  Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292–296. [PMID: 13686342]
4.  Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217–223. [PMID: 3883995]
5.  Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319–326. [PMID: 3277621]
6.  Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144–4151. [DOI] [PMID: 12837789]
[EC 1.1.1.25 created 1961, modified 1976, modified 2004, modified 2021]
 
 
EC 1.1.1.282     
Accepted name: quinate/shikimate dehydrogenase [NAD(P)+]
Reaction: (1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): YdiB; quinate/shikimate dehydrogenase (ambiguous)
Systematic name: L-quinate:NAD(P)+ 3-oxidoreductase
Comments: This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463–19472. [DOI] [PMID: 12637497]
2.  Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176–19182. [DOI] [PMID: 12624088]
[EC 1.1.1.282 created 2004, modified 2021]
 
 
EC 1.1.5.8     
Accepted name: quinate/shikimate dehydrogenase (quinone)
Reaction: quinate + quinone = 3-dehydroquinate + quinol
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): NAD(P)+-independent quinate dehydrogenase; quinate:pyrroloquinoline-quinone 5-oxidoreductase; quinate dehydrogenase (quinone)
Systematic name: quinate:quinol 3-oxidoreductase
Comments: The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-99-5
References:
1.  van Kleef, M.A.G. and Duine, J.A. Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein. Arch. Microbiol. 150 (1988) 32–36. [PMID: 3044290]
2.  Adachi, O., Tanasupawat, S., Yoshihara, N., Toyama, H. and Matsushita, K. 3-Dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway. Biosci. Biotechnol. Biochem. 67 (2003) 2124–2131. [DOI] [PMID: 14586099]
3.  Vangnai, A.S., Toyama, H., De-Eknamkul, W., Yoshihara, N., Adachi, O. and Matsushita, K. Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase. FEMS Microbiol. Lett. 241 (2004) 157–162. [DOI] [PMID: 15598527]
[EC 1.1.5.8 created 1992 as EC 1.1.99.25, modified 2004, transferred 2010 to EC 1.1.5.8, modified 2021]
 
 
EC 1.1.99.25      
Transferred entry: quinate dehydrogenase (pyrroloquinoline-quinone). Now EC 1.1.5.8, quinate dehydrogenase (quinone)
[EC 1.1.99.25 created 1992, modified 2004, deleted 2010]
 
 
EC 1.3.1.12     
Accepted name: prephenate dehydrogenase
Reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): hydroxyphenylpyruvate synthase; chorismate mutase—prephenate dehydrogenase
Systematic name: prephenate:NAD+ oxidoreductase (decarboxylating)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-92-2
References:
1.  Koch, G.L.E., Shaw, D.C. and Gibson, F. Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase. Biochim. Biophys. Acta 212 (1970) 375–386. [DOI] [PMID: 5456988]
[EC 1.3.1.12 created 1972]
 
 
EC 1.3.1.28     
Accepted name: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
Reaction: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH + H+
For diagram of shikimate and chorismate biosynthesis, click here
Other name(s): 2,3-DHB dehydrogenase; 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
Systematic name: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-40-1
References:
1.  Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401–411. [DOI] [PMID: 4306838]
[EC 1.3.1.28 created 1972 as EC 1.1.1.109, transferred 1976 to EC 1.3.1.28]
 
 
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
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
References:
1.  Van Lanen, S.G., Lin, S. and Shen, B. Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism. Proc. Natl. Acad. Sci. USA 105 (2008) 494–499. [DOI] [PMID: 18182490]
2.  Yu, L., Mah, S., Otani, T. and Dedon, P. The benzoxazolinate of C-1027 confers intercalative DNA binding. J. Am. Chem. Soc. 117 (1995) 8877–8878. [DOI]
[EC 1.3.8.16 created 2008 as 1.3.99.24, transferred 2020 to EC 1.3.8.16.]
 
 
EC 1.3.99.24      
Transferred entry: 2-amino-4-deoxychorismate dehydrogenase. Now EC 1.3.8.16, 2-amino-4-deoxychorismate dehydrogenase
[EC 1.3.99.24 created 2008, deleted 2020]
 
 
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
References:
1.  Jiang, M., Cao, Y., Guo, Z.F., Chen, M., Chen, X. and Guo, Z. Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity. Biochemistry 46 (2007) 10979–10989. [DOI] [PMID: 17760421]
[EC 2.2.1.9 created 2008 (EC 2.5.1.64 created 2003, part-incorporated 2008)]
 
 
EC 2.4.2.18     
Accepted name: anthranilate phosphoribosyltransferase
Reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-α-D-ribose 1-diphosphate
For diagram of tryptophan biosynthesis, click here
Other name(s): phosphoribosyl-anthranilate pyrophosphorylase; PRT; anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase; anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase; phosphoribosylanthranilate pyrophosphorylase; phosphoribosylanthranilate transferase; anthranilate-PP-ribose-P phosphoribosyltransferase
Systematic name: N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-α-D-ribosyltransferase
Comments: In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate 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: 9059-35-2
References:
1.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
2.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653]
3.  Ito, J. and Yanofsky, C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J. Bacteriol. 97 (1969) 734–742. [PMID: 4886290]
4.  Wegman, J. and DeMoss, J.A. The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa. J. Biol. Chem. 240 (1965) 3781–3788. [PMID: 5842052]
[EC 2.4.2.18 created 1972]
 
 
EC 2.5.1.19     
Accepted name: 3-phosphoshikimate 1-carboxyvinyltransferase
Reaction: phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Other name(s): 5-enolpyruvylshikimate-3-phosphate synthase; 3-enolpyruvylshikimate 5-phosphate synthase; 3-enolpyruvylshikimic acid-5-phosphate synthetase; 5′-enolpyruvylshikimate-3-phosphate synthase; 5-enolpyruvyl-3-phosphoshikimate synthase; 5-enolpyruvylshikimate-3-phosphate synthetase; 5-enolpyruvylshikimate-3-phosphoric acid synthase; enolpyruvylshikimate phosphate synthase; EPSP synthase
Systematic name: phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-73-9
References:
1.  Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82–90. [PMID: 4289188]
[EC 2.5.1.19 created 1976, modified 1983, modified 1989]
 
 
EC 2.5.1.54     
Accepted name: 3-deoxy-7-phosphoheptulonate synthase
Reaction: phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Other name(s): 2-dehydro-3-deoxy-phosphoheptonate aldolase; 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase; 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase; 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); D-erythrose-4-phosphate-lyase; D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating); DAH7-P synthase; DAHP synthase; DS-Co; DS-Mn; KDPH synthase; KDPH synthetase; deoxy-D-arabino-heptulosonate-7-phosphate synthetase; phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptanoate aldolase; phospho-2-keto-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonic aldolase; phospho-2-oxo-3-deoxyheptonate aldolase
Systematic name: phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-94-2
References:
1.  Srinivasan, P.R. and Sprinson, D.B. 2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase. J. Biol. Chem. 234 (1959) 716–722. [PMID: 13654249]
2.  Jossek, R., Bongaerts, J. and Sprenger, G.A. Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli. FEMS Microbiol. Lett. 202 (2001) 145–148. [DOI] [PMID: 11506923]
3.  Schneider, T.R., Hartmann, M. and Braus, G.H. Crystallization and preliminary X-ray analysis of D-arabino-heptulosonate-7-phosphate synthase (tyrosine inhibitable) from Saccharomyces cerevisiae. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1586–1588. [PMID: 10489454]
[EC 2.5.1.54 created 1965 as EC 4.1.2.15, modified 1976, transferred 2002 to EC 2.5.1.54]
 
 
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 2.5.1.64 created 2003, deleted 2008]
 
 
EC 2.6.1.85     
Accepted name: aminodeoxychorismate synthase
Reaction: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
For diagram of the late stages of folate biosynthesis, click here
Other name(s): ADC synthase; 4-amino-4-deoxychorismate synthase; PabB; chorismate:L-glutamine amido-ligase (incorrect)
Systematic name: chorismate:L-glutamine aminotransferase
Comments: The enzyme is composed of two parts, PabA and PabB. In the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg2+). PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ye, Q.Z., Liu, J. and Walsh, C.T. p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. USA 87 (1990) 9391–9395. [DOI] [PMID: 2251281]
2.  Viswanathan, V.K., Green, J.M. and Nichols, B.P. Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J. Bacteriol. 177 (1995) 5918–5923. [DOI] [PMID: 7592344]
[EC 2.6.1.85 created 2003 as EC 6.3.5.8, transferred 2007 to EC 2.6.1.85]
 
 
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
References:
1.  Van Lanen, S.G., Lin, S. and Shen, B. Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism. Proc. Natl. Acad. Sci. USA 105 (2008) 494–499. [DOI] [PMID: 18182490]
2.  Yu, L., Mah, S., Otani, T. and Dedon, P. The benzoxazolinate of C-1027 confers intercalative DNA binding. J. Am. Chem. Soc. 117 (1995) 8877–8878. [DOI]
3.  McDonald, M., Mavrodi, D.V., Thomashow, L.S. and Floss, H.G. Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid. J. Am. Chem. Soc. 123 (2001) 9459–9460. [PMID: 11562236]
4.  Laursen, J.B. and Nielsen, J. Phenazine natural products: biosynthesis, synthetic analogues, and biological activity. Chem. Rev. 104 (2004) 1663–1686. [DOI] [PMID: 15008629]
[EC 2.6.1.86 created 2008]
 
 
EC 2.7.1.71     
Accepted name: shikimate kinase
Reaction: ATP + shikimate = ADP + 3-phosphoshikimate
For diagram of shikimate and chorismate biosynthesis, click here
Other name(s): shikimate kinase (phosphorylating); shikimate kinase II
Systematic name: ATP:shikimate 3-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-51-0
References:
1.  Morell, H. and Sprinson, D.B. Shikimate kinase isoenzymes in Salmonella typhimurium. J. Biol. Chem. 243 (1968) 676–677. [PMID: 4866525]
[EC 2.7.1.71 created 1972]
 
 
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
References:
1.  Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401–411. [DOI] [PMID: 4306838]
[EC 3.3.2.1 created 1972]
 
 
EC 3.3.2.13     
Accepted name: chorismatase
Reaction: chorismate + H2O = (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: chorismate = (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylate
Other name(s): chorismate/3,4-dihydroxycyclohexa-1,5-dienoate synthase; fkbO (gene name); rapK (gene name)
Systematic name: chorismate pyruvate-hydrolase
Comments: The enzyme found in several bacterial species is involved in the biosynthesis of macrocyclic polyketides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Andexer, J.N., Kendrew, S.G., Nur-e-Alam, M., Lazos, O., Foster, T.A., Zimmermann, A.S., Warneck, T.D., Suthar, D., Coates, N.J., Koehn, F.E., Skotnicki, J.S., Carter, G.T., Gregory, M.A., Martin, C.J., Moss, S.J., Leadlay, P.F. and Wilkinson, B. Biosynthesis of the immunosuppressants FK506, FK520, and rapamycin involves a previously undescribed family of enzymes acting on chorismate. Proc. Natl. Acad. Sci. USA 108 (2011) 4776–4781. [DOI] [PMID: 21383123]
2.  Juneja, P., Hubrich, F., Diederichs, K., Welte, W. and Andexer, J.N. Mechanistic implications for the chorismatase FkbO based on the crystal structure. J. Mol. Biol. 426 (2014) 105–115. [DOI] [PMID: 24036425]
[EC 3.3.2.13 created 2013]
 
 
EC 3.3.2.15     
Accepted name: trans-2,3-dihydro-3-hydroxyanthranilic acid synthase
Reaction: (2S)-2-amino-4-deoxychorismate + H2O = (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate + pyruvate
For diagram of enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, click here
Glossary: (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate = trans-2,3-dihydro-3-hydroxyanthranilate
Other name(s): isochorismatase (ambiguous); phzD (gene name)
Systematic name: (2S)-2-amino-4-deoxychorismate pyruvate-hydrolase
Comments: Isolated from the bacterium Pseudomonas aeruginosa. Involved in phenazine biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mavrodi, D.V., Bonsall, R.F., Delaney, S.M., Soule, M.J., Phillips, G. and Thomashow, L.S. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J. Bacteriol. 183 (2001) 6454–6465. [DOI] [PMID: 11591691]
2.  Parsons, J.F., Calabrese, K., Eisenstein, E. and Ladner, J.E. Structure and mechanism of Pseudomonas aeruginosa PhzD, an isochorismatase from the phenazine biosynthetic pathway. Biochemistry 42 (2003) 5684–5693. [DOI] [PMID: 12741825]
[EC 3.3.2.15 created 2016]
 
 
EC 4.1.1.48     
Accepted name: indole-3-glycerol-phosphate synthase
Reaction: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
For diagram of tryptophan biosynthesis, click here
Other name(s): indoleglycerol phosphate synthetase; indoleglycerol phosphate synthase; indole-3-glycerophosphate synthase; 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase (cyclizing)
Systematic name: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing; 1-C-(indol-3-yl)glycerol-3-phosphate-forming]
Comments: 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 4.1.3.27 (anthranilate 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: 9031-60-1
References:
1.  Creighton, T.E. and Yanofsky, C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J. Biol. Chem. 241 (1966) 4616–4624. [PMID: 5332729]
2.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653]
[EC 4.1.1.48 created 1972]
 
 
EC 4.1.1.98     
Accepted name: 4-hydroxy-3-polyprenylbenzoate decarboxylase
Reaction: a 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO2
For diagram of ubiquinol biosynthesis, click here
Other name(s): ubiD (gene name); 4-hydroxy-3-solanesylbenzoate decarboxylase; 3-octaprenyl-4-hydroxybenzoate decarboxylase
Systematic name: 4-hydroxy-3-polyprenylbenzoate carboxy-lyase
Comments: The enzyme catalyses a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Leppik, R.A., Young, I.G. and Gibson, F. Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Biochim. Biophys. Acta 436 (1976) 800–810. [DOI] [PMID: 782527]
2.  Gulmezian, M., Hyman, K.R., Marbois, B.N., Clarke, C.F. and Javor, G.T. The role of UbiX in Escherichia coli coenzyme Q biosynthesis. Arch. Biochem. Biophys. 467 (2007) 144–153. [DOI] [PMID: 17889824]
3.  Pfaff, C., Glindemann, N., Gruber, J., Frentzen, M. and Sadre, R. Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase are required for plastoquinone biosynthesis in the cyanobacterium Synechocystis sp. PCC6803. J. Biol. Chem. 289 (2014) 2675–2686. [DOI] [PMID: 24337576]
4.  Lin, F., Ferguson, K.L., Boyer, D.R., Lin, X.N. and Marsh, E.N. Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase. ACS Chem. Biol. 10 (2015) 1137–1144. [DOI] [PMID: 25647642]
5.  Payne, K.A., White, M.D., Fisher, K., Khara, B., Bailey, S.S., Parker, D., Rattray, N.J., Trivedi, D.K., Goodacre, R., Beveridge, R., Barran, P., Rigby, S.E., Scrutton, N.S., Hay, S. and Leys, D. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature 522 (2015) 497–501. [DOI] [PMID: 26083754]
[EC 4.1.1.98 created 2014, modified 2015]
 
 
EC 4.1.3.27     
Accepted name: anthranilate synthase
Reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
For diagram of tryptophan biosynthesis, click here
Other name(s): anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE
Systematic name: chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
Comments: 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)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-59-8
References:
1.  Baker, T. and Crawford, I.P. Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli. J. Biol. Chem. 241 (1966) 5577–5584. [PMID: 5333199]
2.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653]
4.  Ito, J. and Yanofsky, C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J. Bacteriol. 97 (1969) 734–742. [PMID: 4886290]
5.  Zalkin, H. and Kling, D. Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium. Biochemistry 7 (1968) 3566–3573. [PMID: 4878701]
[EC 4.1.3.27 created 1972]
 
 
EC 4.1.3.38     
Accepted name: aminodeoxychorismate lyase
Reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
For diagram of the late stages of folate biosynthesis, click here
Other name(s): enzyme X; 4-amino-4-deoxychorismate lyase; 4-amino-4-deoxychorismate pyruvate-lyase
Systematic name: 4-amino-4-deoxychorismate pyruvate-lyase (4-aminobenzoate-forming)
Comments: A pyridoxal-phosphate protein. Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 2.6.1.85, aminodeoxychorismate synthase, to form p-aminobenzoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 132264-33-6
References:
1.  Ye, Q.Z., Liu, J. and Walsh, C.T. p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. USA 87 (1990) 9391–9395. [DOI] [PMID: 2251281]
2.  Green, J.M., Merkel, W.K. and Nichols, B.P. Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J. Bacteriol. 174 (1992) 5317–5323. [DOI] [PMID: 1644759]
3.  Nakai, T., Mizutani, H., Miyahara, I., Hirotsu, K., Takeda, S., Jhee, K.H., Yoshimura, T. and Esaki, N. Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli. J. Biochem. 128 (2000) 29–38. [PMID: 10876155]
[EC 4.1.3.38 created 2003]
 
 
EC 4.1.3.40     
Accepted name: chorismate lyase
Reaction: chorismate = 4-hydroxybenzoate + pyruvate
For diagram of ubiquinol biosynthesis, click here
Other name(s): CL; CPL; UbiC
Systematic name: chorismate pyruvate-lyase (4-hydroxybenzoate-forming)
Comments: This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria [1]. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 157482-18-3
References:
1.  Nichols, B.P. and Green, J.M. Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. J. Bacteriol. 174 (1992) 5309–5316. [DOI] [PMID: 1644758]
2.  Siebert, M., Severin, K. and Heide, L. Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase. Microbiology 140 (1994) 897–904. [DOI] [PMID: 8012607]
3.  Meganathan, R. Ubiquinone biosynthesis in microorganisms. FEMS Microbiol. Lett. 203 (2001) 131–139. [DOI] [PMID: 11583838]
[EC 4.1.3.40 created 2007]
 
 
EC 4.1.3.45     
Accepted name: 3-hydroxybenzoate synthase
Reaction: chorismate = 3-hydroxybenzoate + pyruvate
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: chorismate = (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylate
Other name(s): chorismatase/3-hydroxybenzoate synthase; hyg5 (gene name); bra8 (gene name); XanB2
Systematic name: chorismate pyruvate-lyase (3-hydroxybenzoate-forming)
Comments: The enzyme, found in several bacterial species is involved in biosynthesis of secondary products. The enzyme from the bacterium Xanthomonas campestris pv. campestris also has the activity of EC 4.1.3.40, chorismate lyase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Andexer, J.N., Kendrew, S.G., Nur-e-Alam, M., Lazos, O., Foster, T.A., Zimmermann, A.S., Warneck, T.D., Suthar, D., Coates, N.J., Koehn, F.E., Skotnicki, J.S., Carter, G.T., Gregory, M.A., Martin, C.J., Moss, S.J., Leadlay, P.F. and Wilkinson, B. Biosynthesis of the immunosuppressants FK506, FK520, and rapamycin involves a previously undescribed family of enzymes acting on chorismate. Proc. Natl. Acad. Sci. USA 108 (2011) 4776–4781. [DOI] [PMID: 21383123]
2.  Jiang, Y., Wang, H., Lu, C., Ding, Y., Li, Y. and Shen, Y. Identification and characterization of the cuevaene A biosynthetic gene cluster in Streptomyces sp. LZ35. ChemBioChem 14 (2013) 1468–1475. [DOI] [PMID: 23824670]
3.  Zhou, L., Wang, J.Y., Wang, J., Poplawsky, A., Lin, S., Zhu, B., Chang, C., Zhou, T., Zhang, L.H. and He, Y.W. The diffusible factor synthase XanB2 is a bifunctional chorismatase that links the shikimate pathway to ubiquinone and xanthomonadins biosynthetic pathways. Mol. Microbiol. 87 (2013) 80–93. [DOI] [PMID: 23113660]
[EC 4.1.3.45 created 2013]
 
 
EC 4.2.1.10     
Accepted name: 3-dehydroquinate dehydratase
Reaction: 3-dehydroquinate = 3-dehydroshikimate + H2O
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram). The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering.
Other name(s): 3-dehydroquinate hydrolase; DHQase; dehydroquinate dehydratase; 3-dehydroquinase; 5-dehydroquinase; dehydroquinase; 5-dehydroquinate dehydratase; 5-dehydroquinate hydro-lyase; 3-dehydroquinate hydro-lyase
Systematic name: 3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-66-2
References:
1.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid by 5-dehydroquinase. Biochim. Biophys. Acta 15 (1954) 54–61. [DOI] [PMID: 13198937]
2.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693]
[EC 4.2.1.10 created 1961, modified 1976]
 
 
EC 4.2.1.20     
Accepted name: tryptophan synthase
Reaction: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O (overall reaction)
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
(1b) L-serine + indole = L-tryptophan + H2O
For diagram of tryptophan biosynthesis, click here
Other name(s): L-tryptophan synthetase; indoleglycerol phosphate aldolase; tryptophan desmolase; tryptophan synthetase; L-serine hydro-lyase (adding indoleglycerol-phosphate); L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate, L-tryptophan and glyceraldehyde-3-phosphate-forming]
Systematic name: L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate, L-tryptophan and D-glyceraldehyde-3-phosphate-forming]
Comments: A pyridoxal-phosphate protein. The α-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the β-subunit where, in the presence of pyridoxal 5′-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the β subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the α unit of EC 4.2.1.20 to form a complex.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-52-2
References:
1.  Crawford, I.P. and Yanofsky, C. On the separation of the tryptophan synthetase of Escherichia coli into two protein components. Proc. Natl. Acad. Sci. USA 44 (1958) 1161–1170. [DOI] [PMID: 16590328]
2.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653]
4.  Hyde, C.C., Ahmed, S.A., Padlan, E.A., Miles, E.W. and Davies, D.R. Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263 (1988) 17857–17871. [PMID: 3053720]
5.  Woehl, E. and Dunn, M.F. Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase α-, β-, and αβ-reactions. Biochemistry 38 (1999) 7131–7141. [DOI] [PMID: 10353823]
[EC 4.2.1.20 created 1961, modified 1976, modified 2002, modified 2011]
 
 
EC 4.2.1.51     
Accepted name: prephenate dehydratase
Reaction: prephenate = phenylpyruvate + H2O + CO2
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): prephenate hydro-lyase (decarboxylating)
Systematic name: prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-88-6
References:
1.  Cerutti, P. and Guroff, G. Enzymatic formation of phenylpyruvic acid in Pseudomonas sp. (ATCC 11299A) and its regulation. J. Biol. Chem. 240 (1965) 3034–3048. [PMID: 14342329]
2.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
3.  Schmidt, J.C. and Zalkin, H. Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium. Biochemistry 8 (1969) 174–181. [PMID: 4887851]
[EC 4.2.1.51 created 1972]
 
 
EC 4.2.1.151     
Accepted name: chorismate dehydratase
Reaction: chorismate = 3-[(1-carboxyvinyl)oxy]benzoate + H2O
For diagram of the futalosine pathway, click here
Other name(s): MqnA
Systematic name: chorismate hydro-lyase (3-[(1-carboxyvinyl)oxy]benzoate-forming)
Comments: The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mahanta, N., Fedoseyenko, D., Dairi, T. and Begley, T.P. Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 15318–15321. [DOI] [PMID: 24083939]
[EC 4.2.1.151 created 2014]
 
 
EC 4.2.3.4     
Accepted name: 3-dehydroquinate synthase
Reaction: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram). The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering.
Other name(s): 5-dehydroquinate synthase; 5-dehydroquinic acid synthetase; dehydroquinate synthase; 3-dehydroquinate synthetase; 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing); 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing); 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Systematic name: 3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Comments: Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-77-1
References:
1.  Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669–1672. [DOI] [PMID: 5275368]
2.  Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238 (1963) 3176–3182. [PMID: 14085358]
3.  Bender, S.L., Mehdi, S. and Knowles, J.R. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28 (1989) 7555–7560. [PMID: 2514789]
4.  Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394 (1998) 299–302. [DOI] [PMID: 9685163]
[EC 4.2.3.4 created 1978 as EC 4.6.1.3, transferred 2000 to EC 4.2.3.4, modified 2002]
 
 
EC 4.2.3.5     
Accepted name: chorismate synthase
Reaction: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here
Other name(s): 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
Systematic name: 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming)
Comments: Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH·). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-07-0
References:
1.  Gaertner, F.H. and Cole, K.W. Properties of chorismate synthase in Neurospora crassa. J. Biol. Chem. 248 (1973) 4602–4609. [PMID: 4146266]
2.  Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82–90. [PMID: 4289188]
3.  Welch, G.R., Cole, K.W. and Gaertner, F.H. Chorismate synthase of Neurospora crassa: a flavoprotein. Arch. Biochem. Biophys. 165 (1974) 505–518. [DOI] [PMID: 4155270]
4.  Bornemann, S., Lowe, D.J. and Thorneley, R.N. The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate. Biochemistry 35 (1996) 9907–9916. [DOI] [PMID: 8703965]
5.  Bornemann, S., Theoclitou, M.E., Brune, M., Webb, M.R., Thorneley, R.N. and Abell, C. A secondary β deuterium kinetic isotope effect in the chorismate synthase reaction. Bioorg. Chem. 28 (2000) 191–204. [DOI] [PMID: 11034781]
6.  Osborne, A., Thorneley, R.N., Abell, C. and Bornemann, S. Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction. J. Biol. Chem. 275 (2000) 35825–35830. [DOI] [PMID: 10956653]
[EC 4.2.3.5 created 1978 as EC 4.6.1.4, modified 1983, transferred 2000 to EC 4.2.3.5, modified 2002]
 
 
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
References:
1.  Serino, L., Reimmann, C., Baur, H., Beyeler, M., Visca, P. and Haas, D. Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. Mol. Gen. Genet. 249 (1995) 217–228. [PMID: 7500944]
2.  Kerbarh, O., Ciulli, A., Howard, N.I. and Abell, C. Salicylate biosynthesis: overexpression, purification, and characterization of Irp9, a bifunctional salicylate synthase from Yersinia enterocolitica. J. Bacteriol. 187 (2005) 5061–5066. [DOI] [PMID: 16030197]
[EC 4.2.99.21 created 2010]
 
 
EC 4.6.1.4      
Transferred entry: chorismate synthase. Now EC 4.2.3.5, chorismate synthase
[EC 4.6.1.4 created 1978, modified 1983, deleted 2000]
 
 
EC 5.3.1.24     
Accepted name: phosphoribosylanthranilate isomerase
Reaction: N-(5-phospho-β-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
For diagram of tryptophan biosynthesis, click here
Other name(s): PRA isomerase; PRAI; IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5′-phosphoribosylanthranilate isomerase complex); N-(5-phospho-β-D-ribosyl)anthranilate ketol-isomerase
Systematic name: N-(5-phospho-β-D-ribosyl)anthranilate aldose-ketose-isomerase
Comments: 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 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-82-8
References:
1.  Braus, G.H., Luger, K., Paravicini, G., Schmidheini, T., Kirschner, K. and Hütter, R. The role of the TRP1 gene in yeast tryptophan biosynthesis. J. Biol. Chem. 263 (1988) 7868–7875. [PMID: 3286643]
2.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [DOI] [PMID: 3535653]
[EC 5.3.1.24 created 1990]
 
 
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
References:
1.  Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401–411. [DOI] [PMID: 4306838]
2.  van Tegelen, L.J., Moreno, P.R., Croes, A.F., Verpoorte, R. and Wullems, G.J. Purification and cDNA cloning of isochorismate synthase from elicited cell cultures of Catharanthus roseus. Plant Physiol. 119 (1999) 705–712. [PMID: 9952467]
3.  Dahm, C., Müller, R., Schulte, G., Schmidt, K. and Leistner, E. The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1425 (1998) 377–386. [DOI] [PMID: 9795253]
4.  Daruwala, R., Kwon, O., Meganathan, R. and Hudspeth, M.E. A new isochorismate synthase specifically involved in menaquinone (vitamin K2) biosynthesis encoded by the menF gene. FEMS Microbiol. Lett. 140 (1996) 159–163. [PMID: 8764478]
[EC 5.4.4.2 created 1972 as EC 5.4.99.6, transferred 2003 to EC 5.4.4.2]
 
 
EC 5.4.99.5     
Accepted name: chorismate mutase
Reaction: chorismate = prephenate
For diagram of phenylalanine and tyrosine biosynthesis, click here and for mechanism of reaction, click here
Other name(s): hydroxyphenylpyruvate synthase
Systematic name: chorismate pyruvatemutase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-30-8
References:
1.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
2.  Lorence, J.H. and Nester, E.W. Multiple molecular forms of chorismate mutase in Bacillus subtillis. Biochemistry 6 (1967) 1541–1543. [PMID: 4962500]
3.  Sprössler, B. and Lingens, F. Chorismat-Mutase aus Claviceps. I. Eigenschaften der Chorismat-Mutase aus verschiedenen Claviceps-Stämmen. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 448–458. [PMID: 5443801]
4.  Woodin, T.S. and Nishioka, L. Evidence for three isozymes of chorismate mutase in alfalfa. Biochim. Biophys. Acta 309 (1973) 211–223. [DOI] [PMID: 4708674]
[EC 5.4.99.5 created 1972]
 
 
EC 5.4.99.6      
Transferred entry: isochorismate synthase. Now EC 5.4.4.2, isochorismate synthase
[EC 5.4.99.6 created 1972, deleted 2003]
 
 
EC 5.4.99.67     
Accepted name: 4-amino-4-deoxychorismate mutase
Reaction: 4-amino-4-deoxychorismate = 4-amino-4-deoxyprephenate
Other name(s): cmlD (gene name); papB (gene name)
Systematic name: 4-amino-4-deoxychorismate pyruvatemutase
Comments: The enzyme, characterized from the bacteria Streptomyces venezuelae and Streptomyces pristinaespiralis, participates in the biosynthesis of the antibiotics chloramphenicol and pristinamycin IA, respectively. cf. EC 5.4.99.5, chorismate mutase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Blanc, V., Gil, P., Bamas-Jacques, N., Lorenzon, S., Zagorec, M., Schleuniger, J., Bisch, D., Blanche, F., Debussche, L., Crouzet, J. and Thibaut, D. Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. Mol. Microbiol. 23 (1997) 191–202. [PMID: 9044253]
2.  He, J., Magarvey, N., Piraee, M. and Vining, L.C. The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a monomodular non-ribosomal peptide synthetase gene. Microbiology 147 (2001) 2817–2829. [PMID: 11577160]
[EC 5.4.99.67 created 2019]
 
 
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]
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
References:
1.  Gehring, A.M., Bradley, K.A. and Walsh, C.T. Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 36 (1997) 8495–8503. [DOI] [PMID: 9214294]
2.  Wyckoff, E.E., Stoebner, J.A., Reed, K.E. and Payne, S.M. Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of genes required for early steps in siderophore biosynthesis. J. Bacteriol. 179 (1997) 7055–7062. [PMID: 9371453]
3.  Ehmann, D.E., Shaw-Reid, C.A., Losey, H.C. and Walsh, C.T. The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Proc. Natl. Acad. Sci. USA 97 (2000) 2509–2514. [DOI] [PMID: 10688898]
4.  Keating, T.A., Marshall, C.G. and Walsh, C.T. Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase homologous to nonribosomal peptide synthetase condensation domains. Biochemistry 39 (2000) 15513–15521. [PMID: 11112537]
5.  May, J.J., Wendrich, T.M. and Marahiel, M.A. The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276 (2001) 7209–7217. [DOI] [PMID: 11112781]
6.  Sikora, A.L., Wilson, D.J., Aldrich, C.C. and Blanchard, J.S. Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli. Biochemistry 49 (2010) 3648–3657. [DOI] [PMID: 20359185]
7.  Khalil, S. and Pawelek, P.D. Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-protein interaction between Escherichia coli 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase (EntE). Biochemistry 50 (2011) 533–545. [DOI] [PMID: 21166461]
[EC 6.2.1.71 created 2021 (EC 2.7.7.58 created 1992, incorporated 2021)]
 
 
EC 6.3.5.8      
Transferred entry: aminodeoxychorismate synthase. Now EC 2.6.1.85, aminodeoxychorismate synthase. As ATP is not hydrolysed during the reaction, the classification of the enzyme as a ligase was incorrect
[EC 6.3.5.8 created 2003, deleted 2007]
 
 


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