Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae.

Ishihara K., Yamamoto H., Mitsuhashi K., Nishikawa K., Tsuboi S., Tsuji H., Nakajima N.

An NADPH-dependent alpha-keto amide reductase was purified from Saccharomyces cerevisiae. The molecular mass of the native enzyme was estimated to be 33 and 36 kDa by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The purified enzyme showed a reducing activity not only for aromatic alpha-keto amides but also for aliphatic and aromatic alpha-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.

Biosci. Biotechnol. Biochem. 68:2306-2312(2004) [PubMed] [Europe PMC]

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again