Affiliation:
1. Department of Bacteriology and Immunology and the Department of Biological Chemistry, Harward Medical School, Boston, Massachusetts 02115
Abstract
A nicotinamide adenine dinucleotide-linked dehydrogenase has been partially purified from a mutant of
Escherichia coli
K-12 able to grow on
l
-1,2-propanediol as carbon and energy source. This enzyme catalyzes the dehydrogenation at carbon 1 of
l
-1,2-propanediol, glycerol, 1,3-propanediol, ethylene glycol, and ethyl alcohol. The purified protein requires added ferrous or managanous ions. The
V
max
and the apparent
K
m
for a given substrate vary with the particular metal used.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
90 articles.
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