Worrapoj OonanantJeerus SucharitakulJirundon YuvaniyamaPimchai ChaiyenMahidol UniversityChulalongkorn University2018-06-212018-06-212005-12-01Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.61, No.3 (2005), 312-31417443091174430912-s2.0-33646478150https://repository.li.mahidol.ac.th/handle/20.500.14594/162612-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. © 2005 International Union of Crystallography. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyPhysics and AstronomyCrystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1ArticleSCOPUS10.1107/S1744309105004367