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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/16261
Title: Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1
Authors: Worrapoj Oonanant
Jeerus Sucharitakul
Jirundon Yuvaniyama
Pimchai Chaiyen
Mahidol University
Chulalongkorn University
Keywords: Biochemistry, Genetics and Molecular Biology;Physics and Astronomy
Issue Date: 1-Dec-2005
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.61, No.3 (2005), 312-314
Abstract: 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. © 2005 International Union of Crystallography. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33646478150&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/16261
ISSN: 17443091
17443091
Appears in Collections:Scopus 2001-2005

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