Formate dehydrogenase
نویسندگان
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 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 کاملKinetics for Formate Dehydrogenase of Escherichia coli
Kinetic parameters of the selenium-containing, formate dehydrogenase component of the Escherichia coli formate-hydrogenlyase complex have been determined with purified enzyme. A ping-pong Bi Bi kinetic mechanism was observed. The K,,, for formate is 26 mM, and the K,,, for the electron-accepting dye, benzyl viologen, is in the range 1-5 mM. The maximal turnover rate for the formate-dependent ca...
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...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1990
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1990.tb04940.x