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PMID: 197059 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Kinase replacement by a dehydrogenase for Escherichia coli glycerol utilization.

Journal of bacteriology ·Vol. 131 ·No. 3 ·1977-09-00 ·Pages 1026-8

St Martin EJ, Freedberg WB, Lin EC

Abstract

A mutant of Escherichia coli that employs a glycerol:nicotinamide adenine dinucleotide 2-oxidoreductase (EC 1.1.1.6), instead of adenosine 5'-triphosphate:glycerol 3-phosphotransferase (EC 2.7.1.30), as the first enzyme for the dissimilation of glycerol was constructed. This mutant, like the wild-type strain, still cannot grow anaerobically on glycerol without an exogenous hydrogen acceptor.

MeSH Terms
Aerobiosis Alcohol Oxidoreductases/metabolism Escherichia coli/enzymology,growth & development,metabolism Glycerol/metabolism Glycerol Kinase/metabolism Mutation NAD/metabolism Phosphotransferases/metabolism
Chemicals
NAD Alcohol Oxidoreductases Phosphotransferases Glycerol Kinase Glycerol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
St Martin E J
Freedberg W B
Lin E C
References (15)
15 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.131.3.1026-1028.1977
Published
1977-09-00
Pages
1026-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC235566
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.131.3.1026-1028.1977 PMC Full Text View journal details
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