Synthesis of allitol from D-psicose using ribitol dehydrogenase and formate dehydrogenase
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چکیده
منابع مشابه
Formate dehydrogenase from Ralstonia eutropha
1 Spectroscopic and kinetic properties of the molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. Dimitri Niks, Jayant Duvvuru, Miguel Escalona, and Russ Hille Department of Biochemistry, University of California, Riverside, Riverside, CA 92521 Running title: Formate dehydrogenase from Ralstonia eutropha To whom correspondence should be addressed: Prof. Russ Hil...
متن کاملNAD + -dependent Formate Dehydrogenase from Plants
NAD(+)-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochon...
متن کاملProtein engineering of formate dehydrogenase.
NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) is one of the best enzymes for the purpose of NADH regeneration in dehydrogenase-based synthesis of optically active compounds. Low operational stability and high production cost of native FDHs limit their application in commercial production of chiral compounds. The review summarizes the results on engineering of bacterial and yeast FDHs a...
متن کاملSome properties of formate dehydrogenase.
In addition the enzyme catalyzes the oxidation of NADH by 0 2 . The stoichiometry of the first reaction is proved by the formation of the amount of NADH which under anaerobic conditions exactly corresponds to the amount of formate used. In this reaction NAD is replaceable by a large number of redox dyes. For the second reaction the stoichiometry is proved a) kinetically by the relation of the v...
متن کاملPurification and Characterization of Formate Dehydrogenase
Anaylobacter aguaticus strain KNK607M, which had high NAD-dependent formate dehydrogenase (FDH) activity, was newly isolated. The enzyme, purified to homogeneity, was a dimer composed of identical subunits with a molecular mass of 44 kDa. The specific activity was 9.5 ulmg, and the enzyme was optimum at pH 6.3 and 500C, most stabte at pH 7.0, and stable at 50"C or lovver. The apparent K. yalues...
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ژورنال
عنوان ژورنال: Tropical Journal of Pharmaceutical Research
سال: 2017
ISSN: 1596-9827,1596-5996
DOI: 10.4314/tjpr.v15i12.23