JOURNAL ARTICLE

Kinase replacement by a dehydrogenase for Escherichia coli glycerol utilization

E J St MartinWilliam B. FreedbergEn-Sheng Lin

Year: 1977 Journal:   Journal of Bacteriology Vol: 131 (3)Pages: 1026-1028   Publisher: American Society for Microbiology

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.

Keywords:
Glycerol kinase Glycerol Escherichia coli Biology Biochemistry Nicotinamide adenine dinucleotide Phosphotransferase Oxidoreductase Adenosine triphosphate Mutant Dehydrogenase Enzyme NAD+ kinase Gene

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0.40
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15
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0.53
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Citation History

Topics

Microbial Metabolic Engineering and Bioproduction
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
Fungal and yeast genetics research
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
Protein Structure and Dynamics
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology

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