We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A novel NADP<sup>+</sup>-dependentl-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols.
- Authors
Kataoka, M.; Nakamura, Y.; Urano, N.; Ishige, T.; Shi, G.; Kita, S.; Sakamoto, K.; Shimizu, S.
- Abstract
Aim: A novel NADP+-dependentl-1-amino-2-propanol dehydrogenase was isolated from Rhodococcus erythropolis MAK154, and characterized. Methods and Results: The enzyme was inducibly produced on cultivation with aminoalcohols such as 1-amino-2-propanol, 1-amino-2-butanol and 2-aminocyclohexanol. The enzyme catalyses the NADP+-dependent oxidation of several aminoalcohols, and also the NADPH-dependent asymmetric reduction of an aminoketone compound to a double chiral aminoalcohol, d-pseudoephedrine. Amino acid sequence analysis showed that the enzyme might belong to the short-chain dehydrogenase/reductase family. Conclusions: NADP+-dependentl-1-amino-2-propanol dehydrogenase isolated from R. erythropolis MAK154 reversibly catalysed dehydrogenation of aminoalcohols, and exhibited a unique sterospecifity for the reduction reaction. Significance and Impact of the Study: The enzyme is a promising catalyst for the production of double chiral compound, d-pseudoephedrine, from prochiral substrate.
- Subjects
PROPANOLS; NAD(P)H dehydrogenases; DEHYDROGENASES; EPHEDRINE; SYMPATHOMIMETIC agents; MICROBIOLOGY
- Publication
Letters in Applied Microbiology, 2006, Vol 43, Issue 4, p430
- ISSN
0266-8254
- Publication type
Article
- DOI
10.1111/j.1472-765X.2006.01970.x