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PMID:2673038
| Citation |
Welch, RW, Rudolph, FB and Papoutsakis, ET (1989) Purification and characterization of the NADH-dependent butanol dehydrogenase from Clostridium acetobutylicum (ATCC 824). Arch. Biochem. Biophys. 273:309-18 |
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| Abstract |
Two butanol dehydrogenases with different cofactor requirements and different pH ranges have been detected in Clostridium acetobutylicum ATCC 824. The NADH-dependent butanol dehydrogenase (NADH-BDH) was purified to near homogeneity and characterized. One striking feature of the enzyme is that Zn2+ was needed to obtain a significant recovery during purification. The enzyme was a dimer composed of two subunits with subunit molecular mass of 42 kDa and a native molecular mass of 82 +/- 2 kDa. The kinetics were studied in the direction of the reduction of butyraldehyde. Inhibition studies with S-NADH and butanol indicate that the NADH-BDH follows an ordered bibi mechanism with kinetic constants of 4.86 s-1, 0.18 mM, and 16 mM for Kcat, KNADH, and Kbutyraldehyde, respectively. Activity in the reverse direction was 50-fold lower than that in the forward direction. The NADH-BDH had higher activity with longer chained aldehydes and was inhibited by metabolites containing an adenine moiety. |
| Links | |
| Keywords |
Alcohol Oxidoreductases/isolation & purification; Alcohol Oxidoreductases/metabolism; Clostridium/enzymology; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Substrate Specificity |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0004022: alcohol dehydrogenase (NAD) activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0004022: alcohol dehydrogenase (NAD) activity |
ECO:0000314: |
F |
Table 3 shows enzyme activity with addition of different metabolites |
complete | ||||
See also
References
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