Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions
Author(s) -
Vladimir Leskovac,
Svetlana Trivić,
Draginja Peričin
Publication year - 2003
Publication title -
journal of the serbian chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.227
H-Index - 45
eISSN - 1820-7421
pISSN - 0352-5139
DOI - 10.2298/jsc0302077l
Subject(s) - isomerization , alcohol dehydrogenase , chemistry , nad+ kinase , reaction rate constant , catalysis , cofactor , yeast , alcohol , enzyme , ethanol , equilibrium constant , alcohol oxidoreductase , photochemistry , stereochemistry , computational chemistry , kinetics , organic chemistry , biochemistry , physics , quantum mechanics
In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD + , at pH 7.0, 25 oC, have been esti- mated. The determination of the individual rate constants was achieved by fitting the reac- tion progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD + com-
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom