Unknown

Dataset Information

0

Membrane-bound lactate dehydrogenases and mandelate dehydrogenases of Acinetobacter calcoaceticus. Location and regulation of expression.


ABSTRACT: Acinetobacter calcoaceticus possesses an L(+)-lactate dehydrogenase and a D(-)-lactate dehydrogenase. Results of experiments in which enzyme activities were measured after growth of bacteria in different media indicated that the two enzymes were co-ordinately induced by either enantiomer of lactate but not by pyruvate, and repressed by succinate or L-glutamate. The two lactate dehydrogenases have very similar properties to L(+)-mandelate dehydrogenase and D(-)-mandelate dehydrogenase. All four enzymes are NAD(P)-independent and were found to be integral components of the cytoplasmic membrane. The enzymes could be solubilized in active form by detergents; Triton X-100 or Lubrol PX were particularly effective D(-)-Lactate dehydrogenase and D(-)-mandelate dehydrogenase could be selectively solubilized by the ionic detergents cholate, deoxycholate and sodium dodecyl sulphate.

SUBMITTER: Allison N 

PROVIDER: S-EPMC1144902 | BioStudies | 1985-01-01

SECONDARY ACCESSION(S): 10.1042/bj2270753

REPOSITORIES: biostudies

Similar Datasets

1985-01-01 | S-EPMC1152761 | BioStudies
1987-01-01 | S-EPMC1148630 | BioStudies
1983-01-01 | S-EPMC1154104 | BioStudies
1993-01-01 | S-EPMC1132387 | BioStudies
1998-01-01 | S-EPMC1219563 | BioStudies
1972-01-01 | S-EPMC1174542 | BioStudies
1966-01-01 | S-EPMC1270079 | BioStudies
1968-01-01 | S-EPMC1198693 | BioStudies
1993-01-01 | S-EPMC1134382 | BioStudies
1972-01-01 | S-EPMC1174541 | BioStudies