Catalytic Properties of Alcohol Dehydrogenase fromLeuconostoc mesenteroides
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چکیده
منابع مشابه
A triphosphopyridine nucleotide dependent alcohol dehydrogenase from Leuconostoc mesenteroides.
Ethanol formation during glucose fermentation is a relatively common activity of microorganisms; a few species, including Leuconostoc mesenterodes, produce ethanol as a major fermentation end product. The significant results from experiments with various species on this subject are: (1) at least three different metabolic pathways are available for anaerobic conversion of glucose to ethanol (Kos...
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The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparent k(cat)/K(m) and K(i) values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k(cat)/K(m) value of 788 x 10(4) M...
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The pathways for degradation of 6-phosphogluconate have been rather clearly defined for several organisms, the most notable of which are yeast (Horecker, 1953), Escherichia coli (Cohen, 1951), Pseudomonas saccharophila (Entner and Doudoroff, 1952; MacGee and Doudoroff, 1954), and Pseudomonas fluorescens (Kovachevich and Wood, 1954). The enzymes from yeast and E. coli appear to be similar, if no...
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Glucose 6-phosphate dehydrogenase from Zeuconostoc mesenteroides, previously isolated in crystalline form (Olive, C., and Levy, H. R., Biochemistry, 6, 730 (1967)), is shown to be essentially homogeneous by disc gel electrophoresis and sedimentation velocity analysis. The weight average molecular weight is 103,700, determined by both high speed and low speed sedimentation equilibrium techniques...
متن کاملQuantifying the inactivation rate constants for the molecular species comprising the catalytic cycle of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
When an unstable enzyme is incubated with its substrate(s), catalysis may cease before chemical equilibrium is attained. The residual substrate concentrations depend on their initial concentrations, the initial enzymic activity, and the inactivation rate constants for each molecular species that comprise the catalytic cycle. The underlying theory has been elaborated previously for single-substr...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1971
ISSN: 0002-1369
DOI: 10.1080/00021369.1971.10860073