Open AccessPurification and characterization of malate dehydrogenase from the syntrophic propionate‐oxidizing bacterium strain MPOB
Author(s) -
Kuijk Bernardina L.M.,
Stams Alfons J.M.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08520.x
Subject(s) - citrate synthase , malate dehydrogenase , biochemistry , propionate , enzyme , bacteria , dehydrogenase , biology , nad+ kinase , chemistry , genetics
Malate dehydrogenase from the syntrophic propionate‐oxidizing bacterium strain MPOB was purified 42‐fold. The native enzyme had an apparent molecular mass of 68 kDa and consisted of two subunits of 35 kDa. The enzyme exhibited maximum activity with oxaloacetate at pH 8.5 and 60 °C. The K m for oxaloacetate was 50 μM and for NADH 30 μM. The K m values for l‐malate and NAD were 4 and 1.1 mM, respectively. Substrate inhibition was found at oxaloacetate concentrations higher than 250 μM. The N‐terminal amino acid sequence of the enzyme was similar to the sequences of a variety of other malate dehydrogenases from plants, animals and micro‐organisms.