Stereochemistry of the hydrogen transfer to NAD catalyzed by (S)alanine dehydrogenase from Bacillus subtilis.
Biochimica et biophysica acta
confidence
Key findings
Stereochemistry study of hydrogen transfer to NAD by (S)alanine dehydrogenase; label at C-4 of NADH was exclusively (R) position, classifying the enzyme as A-type.
View source on PubMed (PMID 167853) ↗
- Population
- In vitro enzymatic study using (S)alanine dehydrogenase from Bacillus subtilis
- Blinding
- not_reported
- Controls
- none
- Drug class
- coenzyme
Full abstract
The stereochemistry of the hydrogen transfer to NAD catalyzed by (S)alanine dehydrogenase [ (S)alanine: NAD oxidoreductase (EC 1.4.1.1) ] from B. subtilis was investigated. The label at C-2 of (S) [2,3--3H] alanine was enzymatically transferred to NAD, and the [4--3H]NADH produced isolated and the stereochemistry at C-4 investigated. It was found that the label was exclusively located at the (R) position which indicates that (S)alanine dehydrogenase is an A-type enzyme. This result was confirmed in an alternate way by reducing enzymatically [4--3H]NAD with non labeled (S)alanine and (S)alanine dehydrogenase and investigating the stereochemistry of the ]4--3H]NADH produced. As expected, the label was now exclusively located at the (S) position. This proves that (S)alanine dehydrogenase isolated from B. subtilis should be classified as an A-enzyme with regard to the stereochemistry of the hydrogen transfer to NAD.