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Crystallization and preliminary X‐ray crystallographic analysis of 2‐methyl‐3‐hydroxypyridine‐5‐carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA‐1

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2‐Methyl‐3‐hydroxypyridine‐5‐carboxylic acid (MHPC) oxygenase (MHPCO) catalyzes the conversion of an aromatic substrate, MHPC, to an aliphatic compound, α‐(N‐acetylaminomethylene)‐succinic acid, and is involved in the degradation of vitamin B6 by the soil bacterium Pseudomonas sp. MA‐1. Using only FAD as a cofactor, MHPCO is unique in catalyzing hydroxylation and subsequent aromatic ring cleavage without requiring a metal‐ion cofactor. Here, the crystallization of MHPCO is reported together with preliminary X‐ray crystallographic data. An MHPCO crystal obtained by hanging‐drop vapour diffusion diffracted X‐rays to 2.25 Å resolution and belonged to the triclinic space group P1, with four molecules per asymmetric unit.
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Keywords: MHPCO; Pseudomonas sp. MA‐1; aromatic flavoprotein monooxygenase; aromatic ring cleavage; hydroxypyridine

Document Type: Research Article

Publication date: March 1, 2005

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