2z7b
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(New page: 200px<br /><applet load="2z7b" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z7b, resolution 1.900Å" /> '''Crystal Structure o...)
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Revision as of 09:50, 23 January 2008
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Crystal Structure of Mesorhizobium loti 3-hydroxy-2-methylpyridine-4,5-dicarboxylate decarboxylase
Overview
The function of the mlr6791 gene from Mesorhizobium loti MAFF303099 has, been identified. This gene encodes, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate decarboxylase (HMPDdc), an, enzyme involved in the catabolism of pyridoxal 5'-phosphate (Vitamin B6)., This enzyme was overexpressed in Escherichia coli and characterized., HMPDdc is a 26 kDa protein that catalyzes the decarboxylation of, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to, 3-hydroxy-2-methylpyridine-5-carboxylate. The KM and kcat were found to be, 366 muM and 0.6 s-1, respectively. The structure of this enzyme was, determined at 1.9 A resolution using SAD phasing and belongs to the class, II aldolase/adducin superfamily. While the decarboxylation of, hydroxy-substituted benzene rings is a common motif in biosynthesis, the, mechanism of this reaction is still poorly characterized. The structural, studies described here suggest that catalysis of such decarboxylations, proceeds by an aldolase-like mechanism.
About this Structure
2Z7B is a Single protein structure of sequence from Mesorhizobium loti with as ligand. Active as 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase, with EC number 4.1.1.51 Full crystallographic information is available from OCA.
Reference
Gene Identification and Structural Characterization of the Pyridoxal 5'-Phosphate Degradative Protein 3-Hydroxy-2-methylpyridine-4,5-dicarboxylate Decarboxylase from Mesorhizobium loti MAFF303099(,)., Mukherjee T, McCulloch KM, Ealick SE, Begley TP, Biochemistry. 2007 Oct 31;. PMID:17973403
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