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 1.900&Aring;" /> '''Crystal Structure o...)
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==Overview==
==Overview==
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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.
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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 microM 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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17973403 17973403]
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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 Nov 27;46(47):13606-15. Epub 2007 Oct 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17973403 17973403]
[[Category: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase]]
[[Category: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase]]
[[Category: Mesorhizobium loti]]
[[Category: Mesorhizobium loti]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Begley, T.P.]]
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[[Category: Begley, T P.]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
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[[Category: McCulloch, K.M.]]
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[[Category: McCulloch, K M.]]
[[Category: Mukherjee, T.]]
[[Category: Mukherjee, T.]]
[[Category: MN]]
[[Category: MN]]
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[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:50:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:40 2008''

Revision as of 17:00, 21 February 2008


2z7b, resolution 1.900Å

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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 microM 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 Nov 27;46(47):13606-15. Epub 2007 Oct 31. PMID:17973403

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