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PMID: 4306747 Published · ppublish English Journal Article

Ferrous-activated nicotinamide adenine dinucleotide-linked dehydrogenase from a mutant of Escherichia coli capable of growth on 1, 2-propanediol.

Journal of bacteriology ·Vol. 98 ·No. 1 ·1969-04-00 ·Pages 87-95

Sridhara S, Wu TT, Chused TM, Lin EC

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.

MeSH Terms
Centrifugation, Density Gradient Chromatography Escherichia coli/enzymology,metabolism Ethanol/metabolism Glycerol/metabolism Glycols/metabolism Iron/pharmacology Kinetics Manganese/pharmacology Mutation NAD Oxidoreductases/isolation & purification,metabolism Propylene Glycols/metabolism Spectrophotometry
Chemicals
Glycols Propylene Glycols NAD Ethanol Manganese Iron Oxidoreductases Glycerol
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sridhara S
Wu T T
Chused T M
Lin E C
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34 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1969-04-00
Pages
87-95
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC249908
Subset
IM
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