The Enzyme Database

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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 5.3.3.17     
Accepted name: trans-2,3-dihydro-3-hydroxyanthranilate isomerase
Reaction: (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate = (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
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): phzF (gene name); (5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomerase (incorrect)
Systematic name: (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate isomerase
Comments: The enzyme is involved in phenazine biosynthesis. The product probably spontaneously dimerises to 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Parsons, J.F., Song, F., Parsons, L., Calabrese, K., Eisenstein, E. and Ladner, J.E. Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79. Biochemistry 43 (2004) 12427–12435. [DOI] [PMID: 15449932]
2.  Blankenfeldt, W., Kuzin, A.P., Skarina, T., Korniyenko, Y., Tong, L., Bayer, P., Janning, P., Thomashow, L.S. and Mavrodi, D.V. Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens. Proc. Natl. Acad. Sci. USA 101 (2004) 16431–16436. [DOI] [PMID: 15545603]
3.  Parsons, J.F., Calabrese, K., Eisenstein, E. and Ladner, J.E. Structure of the phenazine biosynthesis enzyme PhzG. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2110–2113. [DOI] [PMID: 15502343]
4.  Mavrodi, D.V., Bleimling, N., Thomashow, L.S. and Blankenfeldt, W. The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 184–186. [PMID: 14684924]
5.  Ahuja, E.G., Janning, P., Mentel, M., Graebsch, A., Breinbauer, R., Hiller, W., Costisella, B., Thomashow, L.S., Mavrodi, D.V. and Blankenfeldt, W. PhzA/B catalyzes the formation of the tricycle in phenazine biosynthesis. J. Am. Chem. Soc. 130 (2008) 17053–17061. [DOI] [PMID: 19053436]
[EC 5.3.3.17 created 2011]
 
 


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