A9560
(R)-Aromatic alcohol dehydrogenase, NADP+ dependent from Lactobacillus kefir
lyophilized powder, 1-5 units/mg solid
Synonym(s):
Alcohol: NADP+ oxidoreductase
form
lyophilized powder
specific activity
1-5 units/mg solid
composition
Protein, ~5% Bradford
storage temp.
−20°C
Application
Broad specificity for alcohols and ketones. Highly enantioselective for many (R)-aromatic alcohols.
Chiral selectivity Vr/Vs ≥15 using (R)-and (S)-sec-phenethyl alcohol.
Chiral selectivity Vr/Vs ≥15 using (R)-and (S)-sec-phenethyl alcohol.
Packaging
Packaged under Argon
Physical form
Lyophilized powder containing HEPES, magnesium chloride and dithiothreitol
Other Notes
One unit will oxidize 1.0 μmole of 2-hexanol to 2-hexanone per min at pH 7.8 at 50°C.
Regulatory Information
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Ossama El-Kabbani et al.
Journal of medicinal chemistry, 48(17), 5536-5542 (2005-08-19)
Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site
João R M Almeida et al.
Applied microbiology and biotechnology, 78(6), 939-945 (2008-03-12)
Saccharomyces cerevisiae alcohol dehydrogenases responsible for NADH-, and NADPH-specific reduction of the furaldehydes 5-hydroxymethyl-furfural (HMF) and furfural have previously been identified. In the present study, strains overexpressing the corresponding genes (mut-ADH1 and ADH6), together with a control strain, were compared
A Tani et al.
Applied and environmental microbiology, 66(12), 5231-5235 (2000-12-01)
NADPH-dependent alkylaldehyde reducing enzyme, which was greatly induced by n-hexadecane, from Acinetobacter sp. strain M-1 was purified and characterized. The purified enzyme had molecular masses of 40 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 160 kDa as
Q Ye et al.
Proteins, 44(1), 12-19 (2001-05-17)
Pig aldehyde reductase containing the active site mutation tyrosine(50) to phenylalanine has been crystallized in the presence of the cofactor NADP(H) to a resolution of 2.2 A. This structure clearly shows loss of the tyrosine hydroxyl group and no other
Kazumasa Takenaka et al.
Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology, 14(8), 1972-1975 (2005-08-17)
Carbonyl reductase (CBR) is a cytosolic NADPH-dependent oxidoreductase metabolizing prostaglandins, steroids, quinines, and anthracycline antibiotics. Many experimental studies have shown that CBR plays important roles in the regulation of tumor progression, but clinical significance of CBR status remains unclear. Thus
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