Abstract
The class of pyridine nucleotide-dependent -hydroxyacid oxidative decarboxylases generally catalyze the oxidative decarboxylation of a -hydroxyacid to a ketone and CO2 using NAD(Pt as the oxidant. There are two subclasses based on the metalsdependence of the reaction. Enzymes that have substrates with electron withdrawing substituents in the a- and or y-position generally do not require a metal ion cofactor, an example is 6-phosphogluconate dehydrogenase. Of the remaining enzymes, some require only a divalent metal ion; e.g. malic enzyme, while the others require both a monovalent and a divalent metal ion, for example tartate dehydrogenase.
Protein & Peptide Letters
Title:Pyridine nucleotide-dependent (3-hydroxyacid oxidative decarboxylases: An overview
Volume: 7 Issue: 5
Author(s): William E. Karsten and Paul F. Cook*
Affiliation:
- Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73CJ72
Abstract: The class of pyridine nucleotide-dependent -hydroxyacid oxidative decarboxylases generally catalyze the oxidative decarboxylation of a -hydroxyacid to a ketone and CO2 using NAD(Pt as the oxidant. There are two subclasses based on the metalsdependence of the reaction. Enzymes that have substrates with electron withdrawing substituents in the a- and or y-position generally do not require a metal ion cofactor, an example is 6-phosphogluconate dehydrogenase. Of the remaining enzymes, some require only a divalent metal ion; e.g. malic enzyme, while the others require both a monovalent and a divalent metal ion, for example tartate dehydrogenase.
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Cite this article as:
Karsten E. William and Cook F. Paul*, Pyridine nucleotide-dependent (3-hydroxyacid oxidative decarboxylases: An overview, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207142048
DOI https://dx.doi.org/10.2174/092986650705221207142048 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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