beta-Chloro-L-alanine inhibition of the Escherichia coli alanine-valine transaminase
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منابع مشابه
Active transport in Escherichia coli B membrane vesicles. Differential inactivating effects from the enzymatic oxidation of beta-chloro-L-alanine and beta-chloro-D-alanine.
Isolated membrane vesicles from Escherichia coli B grown on DL-alanine and glycerol carry out amino acid active transport coupled to a membrane-bound D-alanine dehydrogenase (Kaczorowski, G., Shaw, L., Fuentes, M., and Walsh, C. (1975) J. Biol. Chem. 250, 2855). Certain L-amino acids can also energize solute transport by conversion to their D isomers via an alanine reacemase. Both D-chloroalani...
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The pyridoxal form of alanine aminotransferase from pig heart catalyzes the a,/? elimination reaction with 3chloro-L-alanine as the substrate to form equimolar amounts of pyruvate, ammonia, and chloride. The maximum rate of the a,/3 elimination reaction was 2.5 pmol/min/mg at pH 7.0 (25”(Z), approximately 0.5% that of the transamination reaction between L-alanine and 2-oxoglutarate. Time-depend...
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Cell wall-membrane preparations of Escherichia coli, prepared by the ethylenediaminetetraacetic acid-lysozyme method, contain enzymes which catalyze the oxidation of d-alanine and, to a lesser extent, l-alanine into pyruvate and ammonia without the formation of hydrogen peroxide. The kinetic parameters were (i) pH optima of 8.3 to 8.4 for l- and d-alanine and (ii) a K(m) value of 6.6 +/- 0.2 mM...
متن کاملInactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine.
Purified D-amino acid transaminase from Bacillus sphaericus catalyzes an alpha,beta elimination from the D isomer of beta-chloroalanine to yield equivalent amounts of pyruvate, chloride, and ammonia; the L isomer of chloroalanine is not a substrate for this transaminase. During the beta elimination there is a synchronous loss in enzyme activity; the Kinact for beta-chloroalanine was estimated t...
متن کاملD-alanine oxidase form Escherichia coli: localization and induction by L-alanine.
Dialyzed membranes of Escherichia coli prepared by an ethylenediaminetetraacetic acid-lysozyme method catalyze the oxidation of both l-alanine and d-alanine. The specific activities for the oxidations of both d-alanine and l-alanine are increased fivefold when the cells are grown in the presence of either l-alanine or dl-alanine, but are increased only slightly when grown in the presence of d-a...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1985
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.164.3.1350-1352.1985