Publication: Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1
Issued Date
2005-12-01
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17443091
17443091
17443091
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2-s2.0-33646478150
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Mahidol University
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SCOPUS
Bibliographic Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.61, No.3 (2005), 312-314
Suggested Citation
Worrapoj Oonanant, Jeerus Sucharitakul, Jirundon Yuvaniyama, Pimchai Chaiyen Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.61, No.3 (2005), 312-314. doi:10.1107/S1744309105004367 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/16261
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Title
Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1
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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.