Structural highlights
Function
Q988D3_RHILO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A vitamin B(6) degradative pathway has recently been identified and characterized in Mesorhizobium loti MAFF303099. One of the enzymes on this pathway, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO), is a flavin-dependent enzyme and catalyzes the oxidative ring-opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid to form E-2-(acetamino-methylene)succinate. The gene for this enzyme has been cloned, and the corresponding protein has been overexpressed in Escherichia coli and purified. The crystal structure of MHPCO has been solved to 2.1 A using SAD phasing with and without the substrate MHPC bound. These crystal structures provide insight into the reaction mechanism and suggest roles for active site residues in the catalysis of a novel oxidative ring-opening reaction.
Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications.,McCulloch KM, Mukherjee T, Begley TP, Ealick SE Biochemistry. 2009 Apr 1. PMID:19317437[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McCulloch KM, Mukherjee T, Begley TP, Ealick SE. Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications. Biochemistry. 2009 Apr 1. PMID:19317437 doi:10.1021/bi900149f
