Stereospecific d-Glucokinase of Aerobacter aerogenes
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منابع مشابه
D-apiose reductase from Aerobacter aerogenes.
A strain of Aerobacter aerogenes PRL-R3 has been isolated which utilizes d-apiose as its sole source of carbon. A new enzyme, d-apiose reductase, was discovered in this strain. The enzyme was not present when the strain was grown on d-glucose. d-Apiose reductase catalyzes the nicotinamide adenine dinucleotide-dependent interconversion of d-apiose and d-apiitol. The enzyme is specific for d-apio...
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The enzyme D-ribulokinase from Aerobacter aerogenes was purified to near homogeneity. The molecular weight, as determined by Sephacryl gel chromatography, is 116,000. The subunit molecular weight, determined by sodium dodecyl sulfate-gel electrophoresis, is 59,000, suggesting that D-ribulokinase is a dimer of identical subunits. Initial rate kinetic studies, involving substrate analogs and prod...
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Aerobacter aerogenes is noted for its versatility in being capable of growth by utilizing many of the rare and unnatural carbohydrates as substrates. The mechanism of growth on several of these unnatural carbohydrates has been previously reported. A. aerogenes PRL-R3 possesses the ability to synthesize, in response to the common substrate ribitol, a ribitol dehydrogenase which will also catalyz...
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Two pathways for methionine methyl formation, one cobalamindependent and one cobalamin-independent, corresponding to those observed in Escherichia coli PA 15 have been found in Aerobacter aerogenes. An initial difficulty in showing the cobalamin-dependent pathway in cellfree extracts proved to be due to the presence of enzymes which caused the removal of adenosylmethionine, a cofactor required ...
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A capsulated strain of derobacter aerogenes 1033 (2) has been found to metabolize glycerol via two separate pathways. The first pathway was mediated by a diphosphopyridine nucleotidelinked glycerol dehydrogenase and a specific dihydroxyacetone kinase, whereas the second pathway involved a specific glycerol kinase and a DPN-independent L-a-glycerophosphate dehydrogenase (3-5). Although all the a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96893-6