Chirality of the Hydrogen transfer to NAD catalyzed by (3R) hydroxybutyrate dehydrogenase from Pseudomonas lemoignei.
Zeitschrift fur Naturforschung. Section C, Biosciences
confidence
Key findings
Investigated chirality of hydrogen transfer from (3R) hydroxybutyrate to NAD; classified enzyme as B or (S) type dehydrogenase. No clinical/biological endpoints.
View source on PubMed (PMID 201119) ↗
- Sample size
- Not reported
- Population
- In vitro enzymatic study using (3R) hydroxybutyrate dehydrogenase from Pseudomonas lemoignei
- Dosing
- Not reported
- Duration
- Not reported
- Route
- In vitro
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- coenzyme
Full abstract
The chirality of the hydrogen transfer from (3R) hydroxybutyrate to NAD catalyzed by (3R)hydroxybutyrate dehydrogenase (E.C. 1.1.1.30, D-3-hydroxybutyrate : NAD oxidoreductase) from Pseudomonas lemoignei was investigated. [4(-3)H] NAD was enzymatically reduced to (4R) [4(-3)H]NADH with (3RS) hydroxybutyrate. This observation was confirmed since NAD could be reduced to (4S) [4(-3)H] NADH with (3RS) [3(-3)H] hydroxybutyrate and (3R) hydroxybutyrate dehydrogenase. From these experiments it can be concluded that (3R) hydroxybutyrate dehydrogenase from P. lemoignei should be classified as an B or (S) type dehydrogenase.