Premium
A novel NADP + ‐dependent l ‐1‐amino‐2‐propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols
Author(s) -
Kataoka M.,
Nakamura Y.,
Urano N.,
Ishige T.,
Shi G.,
Kita S.,
Sakamoto K.,
Shimizu S.
Publication year - 2006
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.2006.01970.x
Subject(s) - rhodococcus , enzyme , chemistry , bacteria , stereochemistry , biochemistry , biology , genetics
Aim: A novel NADP + ‐dependent l ‐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 + ‐dependent l ‐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.