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3-Dehydro-L-gulonate-6-phosphate decarboxylase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Escherichia Coli Ethylene Glycol Matic Activity Substrate Binding Catabolic Pathway 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.: Homologous (β/α)8-barrel enzymes that catalyze unrelated reactions: orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry, 41, 3861–3869 (2002)CrossRefPubMedGoogle Scholar
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    Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.: Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5′-monophosphate decarboxylase suprafamily. Biochemistry, 42, 12133–12142 (2003)CrossRefPubMedGoogle Scholar
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    Yew, W.S.; Wise, E.L.; Rayment, I.; Gerlt, J.A.: Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry, 43, 6427–6437 (2004)CrossRefPubMedGoogle Scholar
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    Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.: Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry, 43, 6438–6446 (2004)CrossRefPubMedGoogle Scholar
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    Yew, W.S.; Akana, J.; Wise, E.L.; Rayment, I.; Gerlt, J.A.: Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry, 44, 1807–1815 (2005)CrossRefPubMedGoogle Scholar
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    Wise, E.L.; Yew, W.S.; Akana, J.; Gerlt, J.A.; Rayment, I.: 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. Biochemistry, 44, 1816–1823 (2005)CrossRefPubMedGoogle Scholar
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    Yew, W.S.; Gerlt, J.A.: Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol., 184, 302–306 (2002)CrossRefPubMedGoogle Scholar

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