Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

Trans-2,3-dihydro-3-hydroxyanthranilate isomerase (EC 5.3.3.17, phzF (gene)) is an enzyme with systematic name (5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomerase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate

\rightleftharpoons

(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate

The enzyme is involved in phenazine biosynthesis.

References

↑ Parsons, J.F., Song, F., Parsons, L., Calabrese, K., Eisenstein, E. and Ladner, J.E. (2004). "Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79". Biochemistry 43: 12427–12435. doi:10.1021/bi049059z. PMID 15449932.
↑ Blankenfeldt, W., Kuzin, A.P., Skarina, T., Korniyenko, Y., Tong, L., Bayer, P., Janning, P., Thomashow, L.S. and Mavrodi, D.V. (2004). "Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens". Proc. Natl. Acad. Sci. USA 101: 16431–16436. doi:10.1073/pnas.0407371101. PMID 15545603.
↑ Parsons, J.F., Calabrese, K., Eisenstein, E. and Ladner, J.E. (2004). "Structure of the phenazine biosynthesis enzyme PhzG". Acta Crystallogr. D Biol. Crystallogr. 60: 2110–2113. doi:10.1107/s0907444904022474. PMID 15502343.
↑ Mavrodi, D.V., Bleimling, N., Thomashow, L.S. and Blankenfeldt, W. (2004). "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: 184–186. doi:10.1107/s090744490302571x. PMID 14684924.
↑ Ahuja, E.G., Janning, P., Mentel, M., Graebsch, A., Breinbauer, R., Hiller, W., Costisella, B., Thomashow, L.S., Mavrodi, D.V. and Blankenfeldt, W. (2008). "PhzA/B catalyzes the formation of the tricycle in phenazine biosynthesis". J. Am. Chem. Soc. 130: 17053–17061. doi:10.1021/ja806325k. PMID 19053436.

External links

Trans-2,3-dihydro-3-hydroxyanthranilate isomerase at the US National Library of Medicine Medical Subject Headings (MeSH)

Isomerases: intramolecular oxidoreductases (EC 5.3)

5.3.1: Aldoses/Ketoses	Triosephosphate isomerase Ribose-5-phosphate isomerase Mannose phosphate isomerase Glucose isomerase

5.3.2: Keto/Enol	Phenylpyruvate tautomerase Oxaloacetate tautomerase

5.3.3: C = C	Steroid D-isomerase Isopentenyl-diphosphate delta isomerase Vinylacetyl-CoA D-isomerase Muconolactone D-isomerase Cholestenol Delta-isomerase (EBP) Methylitaconate D-isomerase Aconitate Delta-isomerase Enoyl CoA isomerase Prostaglandin-A1 Delta-isomerase 5-carboxymethyl-2-hydroxymuconate D-isomerase Isopiperitenone D-isomerase L-dopachrome isomerase Polyenoic fatty acid isomerase

5.3.4: S-S	Protein disulfide-isomerase (PDIA3)

5.3.99: other	Prostaglandin D2 synthase/Prostaglandin-D synthase Prostaglandin E synthase Prostacyclin synthase Thromboxane-A synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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