Purification and Properties of Cephalosporin-C Deacetylase from the Yeast, Rhodotorula glutinis 38B1, Useful for Bioconversion of 7-Aminocephalosporanic Acid Derivatives

概要

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A 7-aminocephalosporanic acid(7-ACA)deacetylating enzyme sas purified to homogeneity from Rhodotorula glutinis 38B1, whose resting cells have been previously reported as useful for the conversion of 7-ACA derivatives [Sakai et al. , Appl. Environ. Microbiol. , 62, 2667-2672, 1996]. The purified enzyme was a diner comprised of identical subunits with a molecular mass of 82 kDa. The purified enzyme used cephalosporin C and several 7-ACA derivatives with low K_m and high k_<cat> values as substrates, as well as some acetyl esters with relatively long-chain alcohols. Based on this substrate specificity, the enzyme is classified as cephalosporin-C deacetylase(EC 3.1.1.41). The enzyme was most active at 35℃ and pH 5.5, and was inhibited by several serine enzyme inhibitors. The purified enzyme was glycosylated on the addition of an asparaginelinked "hybrid type" oligosaccharide, and most of the enzyme activity was found in the purified cell wall fraction. The enzyme localization and kinetic properties explain the high efficiency of 7-ACA deacetylation in a resting-cell reaction.
社団法人日本生物工学会の論文
1998-01-25