Article
Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus.
The Journal of biological chemistry - 6 Dec 2002
Hektor Harm J, Kloosterman Harm, Dijkhuizen Lubbert
Abstract excerpt
The Bacillus methanolicus methanol dehydrogenase (MDH) is a decameric nicotinoprotein alcohol dehydrogenase (family III) with one Zn(2+) ion, one or two Mg(2+) ions, and a tightly bound cofactor NAD(H) per subunit. The Mg(2+) ions are essential for binding of cofactor NAD(H) in MDH. A B. methanolicus activator protein strongly stimulates the relatively low coenzyme NAD(+)-dependent MDH activity, involving...
Topics
- Alcohol Oxidoreductases
- Amino Acid Sequence
- Bacillus
- Base Sequence
- Binding Sites
- Chromatography, Ion Exchange
- Escherichia coli
- Kinetics
- Models, Chemical
- Molecular Sequence Data
- Mutagenesis, Site-Directed