title: Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1.
abstract: 2-Methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase (MHPCO) catalyzes the conversion of an aromatic substrate, MHPC, to an aliphatic compound, alpha-(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 A resolution and belonged to the triclinic space group P1, with four molecules per asymmetric unit.
authors.affiliation: Department of Biochemistry, Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Phayathai, Bangkok 10400, Thailand.
authors.forename: Worrapoj
authors.initials: W
authors.lastname: Oonanant
authors.forename: Jeerus
authors.initials: J
authors.lastname: Sucharitakul
authors.forename: Jirundon
authors.initials: J
authors.lastname: Yuvaniyama
authors.forename: Pimchai
authors.initials: P
authors.lastname: Chaiyen
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008958:Models, Molecular; D011549:Pseudomonas / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D006899:Mixed Function Oxygenases; C019483:methylhydroxypyridine-carboxylate dioxygenase