Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1.
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.
Oonanant
Worrapoj
W
Department of Biochemistry, Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Phayathai, Bangkok 10400, Thailand.
Sucharitakul
Jeerus
J
Yuvaniyama
Jirundon
J
Chaiyen
Pimchai
P
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
D001426:Bacterial Proteins; D006899:Mixed Function Oxygenases; C019483:methylhydroxypyridine-carboxylate dioxygenase