Open AccessCrystallization and preliminary X‐ray crystallographic analysis of 2‐methyl‐3‐hydroxypyridine‐5‐carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA‐1
Author(s) -
Oonanant Worrapoj,
Sucharitakul Jeerus,
Yuvaniyama Jirundon,
Chaiyen Pimchai
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105004367
Subject(s) - crystallization , x ray , crystallography , chemistry , carboxylic acid , pseudomonas , oxygenase , stereochemistry , polymer chemistry , organic chemistry , physics , biology , enzyme , bacteria , optics , genetics
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 B 6 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 P 1, with four molecules per asymmetric unit.