A long-chain secondary alcohol dehydrogenase from Rhodococcus erythropolis ATCC 4277
Article Abstract:
A secondary alcohol dehydrogenase dependent upon NAD was isolated from Rhodococcus erythropolis ATCC 4277 and appears to catalyze reactions on various substrates, especially long-chain secondary aliphatic alcohols. The enzyme was most active on 2-alcohols with 6 to 12 carbon atoms. It also had specific activity on a particular stereoisomer of 2-octanol. It was considerably less active on primary alcohols than secondary alcohols. The enzyme's kinetic constants and stability at different temperatures is discussed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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Bacillus subtilis vegetative catalase is an extracellular enzyme
Article Abstract:
Bacillus subtilis cells in the stationary growth phase secrete the vegetative catalase KatA when grown in a rich culture medium. The bacteria requires KatA activity to protect itself completely from oxidative stress and H2O2. Cytoplasmic catalase activity alone does not provide protection from oxidative stress. This suggests that the vegetative catalase is an extracellular enzyme rather than an endocellular enzyme. The bacterial cells present in a sporulation-inducing medium do not produce any catalase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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A three-component enzyme system catalyzes the O demethylation of the herbicide dicamba in Pseudomonas maltophilia DI-6
Article Abstract:
An enzyme activity which transforms dicamba (2-methoxy-3,6-dichlorobenzoic acid) to 3,6-dichlorosalicylic acid in vitro was found in cell lysates of Pseudomonas maltophilia DI-6. Phenyl-Sepharose column chromatography of a partially purified lysate caused the separation of this enzyme into three separate protein components tentatively identified as an oxygenase, a ferredoxin and a reductase. The activity of dicamba O-demethylase was affected by oxygen and needed NADH and Mg2+.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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