EC |
1.7.99.1 |
Accepted name: |
hydroxylamine reductase |
Reaction: |
NH3 + H2O + acceptor = hydroxylamine + reduced acceptor |
Other name(s): |
hydroxylamine (acceptor) reductase; ammonia:(acceptor) oxidoreductase |
Systematic name: |
ammonia:acceptor oxidoreductase |
Comments: |
A flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. May be identical to EC 1.7.2.1, nitrite reductase (NO-forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-42-1 |
References: |
1. |
Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F. Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200. |
2. |
Walker, G.C. and Nicholas, D.J.D. Hydroxylamine reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 49 (1961) 361–368. [DOI] [PMID: 13782715] |
3. |
Richter, C.D., Allen, J.W., Higham, C.W., Koppenhofer, A., Zajicek, R.S., Watmough, N.J. and Ferguson, S.J. Cytochrome cd1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme. J. Biol. Chem. 277 (2002) 3093–3100. [DOI] [PMID: 11709555] |
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[EC 1.7.99.1 created 1961, modified 1999, modified 2002] |
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EC |
1.10.3.16 |
Accepted name: |
dihydrophenazinedicarboxylate synthase |
Reaction: |
(1) (1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2 = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2 (2) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2 (3) (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2 (4) (1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-5,10-dihydrophenazine-1-carboxylate + H2O2 |
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For diagram of enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, click here |
Other name(s): |
phzG (gene name) |
Systematic name: |
1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate:oxygen oxidoreductase |
Comments: |
Requires FMN. The enzyme, isolated from the bacteria Pseudomonas fluorescens 2-79 and Burkholderia lata 383, is involved in biosynthesis of the reduced forms of phenazine, phenazine-1-carboxylate, and phenazine-1,6-dicarboxylate, where it catalyses multiple reactions. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Xu, N., Ahuja, E.G., Janning, P., Mavrodi, D.V., Thomashow, L.S. and Blankenfeldt, W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 1403–1413. [DOI] [PMID: 23897464] |
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[EC 1.10.3.16 created 2016] |
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EC |
1.14.13.218 |
Accepted name: |
5-methylphenazine-1-carboxylate 1-monooxygenase |
Reaction: |
5-methylphenazine-1-carboxylate + NADH + O2 = pyocyanin + NAD+ + CO2 + H2O |
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For diagram of enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, click here |
Glossary: |
pyocyanin = 1-hydroxy-5-methylphenazin-5-ium |
Other name(s): |
phzS (gene name) |
Systematic name: |
5-methylphenazine-1-carboxylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating) |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. It can also act on phenazine-1-carboxylate, converting it into phenazin-1-ol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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., Greenhagen, B.T., Shi, K., Calabrese, K., Robinson, H. and Ladner, J.E. Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry 46 (2007) 1821–1828. [DOI] [PMID: 17253782] |
3. |
Greenhagen, B.T., Shi, K., Robinson, H., Gamage, S., Bera, A.K., Ladner, J.E. and Parsons, J.F. Crystal structure of the pyocyanin biosynthetic protein PhzS. Biochemistry 47 (2008) 5281–5289. [DOI] [PMID: 18416536] |
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[EC 1.14.13.218 created 2016] |
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EC |
2.1.1.327 |
Accepted name: |
phenazine-1-carboxylate N-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + phenazine-1-carboxylate = S-adenosyl-L-homocysteine + 5-methylphenazine-1-carboxylate |
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For diagram of enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, click here |
Other name(s): |
phzM (gene name) |
Systematic name: |
S-adenosyl-L-methionine:phenazine-1-carboxylate 5-methyltransferase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Parsons, J.F., Greenhagen, B.T., Shi, K., Calabrese, K., Robinson, H. and Ladner, J.E. Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry 46 (2007) 1821–1828. [DOI] [PMID: 17253782] |
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[EC 2.1.1.327 created 2016] |
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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 |
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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, PDB |
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] |
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[EC 3.3.2.15 created 2016] |
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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 |
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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, PDB |
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] |
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[EC 5.3.3.17 created 2011] |
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