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1xbx

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{{STRUCTURE_1xbx| PDB=1xbx | SCENE= }}
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'''Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound D-ribulose 5-phosphate'''
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===Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound D-ribulose 5-phosphate===
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==Overview==
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3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-hex-3-ulose 6-phosphate synthase (HPS), members of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily, catalyze reactions that involve the formation of Mg(2+)-ion stabilized 1,2-enediolate intermediates. The active sites of KGPDC and HPS share several conserved residues, including the presumed ligands for the Mg(2+) and a catalytic histidine residue that has been implicated in protonation of the intermediate in the KGPDC-catalyzed reaction. As reported in the previous manuscript, both enzymes are naturally promiscuous, with KGPDC from Escherichia coli catalyzing a low level of the HPS reaction and the HPS from Methylomonas aminofaciens catalyzing a significant level of the KGPDC reaction. Interestingly, the promiscuous HPS reaction catalyzed by KGPDC can be significantly enhanced by replacing no more than four active site residues from KGPDC reaction with residues from HPS. In this manuscript, we report structural studies of wild-type and mutant KDGPC's that provide a structural explanation for both the natural promiscuity for the HPS reaction and the enhanced HPS activity and diminished KGPDC activity catalyzed by active site mutants.
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{{ABSTRACT_PUBMED_15697207}}
==About this Structure==
==About this Structure==
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[[Category: Yew, W S.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:59:06 2008''

Revision as of 20:59, 28 July 2008

Image:1xbx.png

Template:STRUCTURE 1xbx

Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound D-ribulose 5-phosphate

Template:ABSTRACT PUBMED 15697207

About this Structure

Full crystallographic information is available from OCA.

Reference

Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I, Biochemistry. 2005 Feb 15;44(6):1816-23. PMID:15697207

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