Enzymatic assay of D-xylose isomerase with D-sorbitol dehydrogenase.
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چکیده
منابع مشابه
Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase.
The mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase suggested from X-ray-crystallographic studies was tested by detailed kinetic analysis of the enzyme with various metal ions at different pH values and temperatures. At D-fructose concentrations used in commercial processes Mg2+ is the best activator with an apparent dissociation constant of 63 microM; Co2+ and Mn2+ bin...
متن کاملCrystallographic studies of D-xylose isomerase.
* This work was supported by National Institutes of Health Grants CA-10925, CA-OG927, and RR-05539 from the United States Public Health Service and by an appropriation from the Commonwealth of Pennsylvania. (I), was crystallized from acetone. The enzyme from Bacillus coagulans has also been crystallized from ammonium sulfate solution and from aqueous acetone (3). We describe here preliminary x-...
متن کاملEnzymatic assay of D-glucuronate using uronate dehydrogenase.
D-Glucuronate is a key metabolite in the process of detoxification of xenobiotics and in a recently constructed synthetic pathway to produce D-glucaric acid, a "top value-added chemical" from biomass. A simple and specific assay of D-glucuronate would be useful for studying these processes, but existing assays are either time-consuming or nonspecific. Using uronate dehydrogenase cloned from Agr...
متن کاملD-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes.
n-Mannitol has been used as a carbon source for the growth of many microorganisms. Some bacteria contain diphosphopyridine nucleotide-dependent dehydrogenases that will oxidize n-mannitol to n-fructose at the nonphosphorylated level (2-5). On the other hand, Wolff and Kaplan (6, 7) have reported the presence of a diphosphopyridine nucleotide-dependent n-mannitol l-phosphate dehydrogenase that o...
متن کاملProperties of D-xylose isomerase from Streptomyces albus.
A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined. D-Glucose, D-xylose, D-ribose, L-arabinose, and L-rhamnose served as substrates for the enzyme with respective Km values of 86, 93, 350, 153, and 312 mM and Vmax values measuring 1.23, 2.9, 2.63, 0.153, and 0.048 mumol min per mg of protein. The h...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1974
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.38.2035