Abstract
Adenosylcobalamin-dependent glycerol dehydratase undergoes inactivation by glycerol, the physiological substrate, during catalysis. In permeabilized cells of Klebsiella pneumoniae, the inactivated enzyme is reactivated in the presence of ATP, Mg2+, and adenosylcobalamin. We identified the two open reading frames as the genes for a reactivating factor for glycerol dehydratase and designated them gdrA and gdrB. The reactivation of the inactivated glycerol dehydratase by the gene products was confirmed in permeabilized recombinant Escherichia coli cells coexpressing GdrA and GdrB proteins with glycerol dehydratase.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins*
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Cell Membrane Permeability
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Cobamides / metabolism*
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Enzyme Activation
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Escherichia coli / genetics
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Genes, Bacterial*
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Glycerol / metabolism
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Hydro-Lyases / genetics*
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Hydro-Lyases / metabolism*
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Klebsiella pneumoniae / enzymology
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Klebsiella pneumoniae / genetics*
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Propylene Glycol / metabolism
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Protein Binding
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Recombinant Proteins / metabolism
Substances
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Bacterial Proteins
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Cobamides
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Recombinant Proteins
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Propylene Glycol
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Hydro-Lyases
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glycerol dehydratase reactivating factor, Klebsiella pneumoniae
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glycerol dehydratase
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cobamamide
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Glycerol