Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase.
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ABSTRACT:
SUBMITTER: Kalliri E
PROVIDER: S-EPMC2395033 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Publications
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase.
Kalliri Efthalia E Mulrooney Scott B SB Hausinger Robert P RP
Journal of bacteriology 20080404 11
YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product alpha-ketoglutaric acid is explained by the very high reduction potential (+19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover alpha-ketoglutarate mistakenly reduced by other enzymes ...[more]
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