Regulation of d -Xylose and d -Arabitol Catabolism by Aerobacter aerogenes
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چکیده
منابع مشابه
An inducible D-arabitol dehydrogenase from Aerobacter aerogenes.
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...
متن کاملGrowth of Aerobacter aerogenes on D-arabinose and L-xylose.
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...
متن کاملD-Arabitol catabolic pathway in Klebsiella aerogenes.
Klebsiella aerogenes strain W70 has an inducible pathway for the degradation of d-arabitol which is comparable to the one found in Aerobacter aerogenes strain PRL-R3. The pathway is also similar to the pathway of ribitol catabolism in that it is composed of a pentitol dehydrogenase, d-arabitol dehydrogenase (ADH), and a pentulokinase, d-xylulokinase (DXK). These two enzymes are coordinately con...
متن کاملD-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...
متن کاملRegulation of myo-inositol catabolism in Aerobacter aerogenes.
A mutant of Aerobacter aerogenes produces constitutively the series of enzymes that mediates the degradation of myo-inositol and which in the wildtype strain is inducible. When grown on l-histidine, the mutant forms the enzymes at a level approximately three times as high as that seen in the induced wild type. The enzymes appear to be coordinately regulated and are sensitive to catabolite repre...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1973
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.113.3.1404-1411.1973