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PMID:7721705
| Citation |
Daniel, R, Boenigk, R and Gottschalk, G (1995) Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli. J. Bacteriol. 177:2151-6 |
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| Abstract |
1,3-Propanediol dehydrogenase (EC 1.1.1.202) was purified to homogeneity from Citrobacter freundii grown anaerobically on glycerol in continuous culture. The enzyme is an octamer of a polypeptide of 43,400 Da. When tested as a dehydrogenase, the enzyme was most active with substrates containing two primary alcohol groups separated by one or two carbon atoms. In the physiological direction, 3-hydroxypropionaldehyde was the preferred substrate. The apparent Km values of the enzyme for 3-hydroxypropionaldehyde and NADH were 140 and 33 microM, respectively. The enzyme was inhibited by chelators of divalent cations but could be reactivated by the addition of Fe2+. The dhaT gene, encoding the 1,3-propanediol dehydrogenase, was cloned, and its nucleotide sequence (1,164 bp) was determined. The deduced dhaT gene product (387 amino acids, 41,324 Da) showed a high level of similarity to a novel family (type III) of alcohol dehydrogenases. The dhaT gene was overexpressed in Escherichia coli 274-fold by using the T7 RNA polymerase/promoter system. |
| Links | |
| Keywords |
Alcohol Dehydrogenase; Alcohol Oxidoreductases/genetics; Alcohol Oxidoreductases/isolation & purification; Alcohol Oxidoreductases/metabolism; Amino Acid Sequence; Base Sequence; Cations, Divalent/pharmacology; Citrobacter freundii/enzymology; Citrobacter freundii/genetics; Cloning, Molecular; DNA, Bacterial/genetics; Enzyme Activation/drug effects; Escherichia coli/genetics; Gene Expression; Genes, Bacterial; Kinetics; Molecular Sequence Data; Molecular Weight; Protein Conformation; Sequence Homology, Amino Acid; Substrate Specificity |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0047516: 1,3-propanediol dehydrogenase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0047516: 1,3-propanediol dehydrogenase activity |
ECO:0000314: |
F |
Table 2: "The activity of 1,3-propanediol dehydrogenase in oxidation reactions was determined spectrophotometrically by the initial rate of substrate- dependent NADH increase" 3-hydroxypropanal and NADH are present as a result of enzyme utilizing 1,3-propanediol (Km values reported) |
complete | ||||
See also
References
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