On the substrate preference of glutaryl acylases

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• 作者：Elena Rosini^a ; ^b ; Claudia Stella Monelli^a ; ^b ; Loredano Pollegioni^a ; ^b ; ^{loredano.pollegioni@uninsubria.it} ; Sergio Riva^b ; ^c ; Daniela Monti^b ; ^c
• 关键词：7-ACA ; 7-aminocephalosporanic acid ; 7-ADCA ; 7-aminodesacetoxycephalosporanic acid ; CA ; cephalosporin C acylase ; CephC ; cephalosporin C ; pDMAB ; p-4-dimethylaminobenzaldehyde ; GA ; glutaryl acylase ; Gl-7-ACA ; glutaryl-7-aminocephalosporanic acid ; Gl-7-ADCA
• 刊名：Journal of Molecular Catalysis B: Enzymatic
• 出版年：2012
• 出版时间：April, 2012
• 年：2012
• 卷：76
• 期：Complete
• 页码：52-58
• 全文大小：640 K

文摘

The substrate preferences of three acylases - two wild-type enzymes and an evolved variant obtained by directed evolution - which are prototypical enzymes for glutaryl-7-ACA acylase and cephalosporin C acylase subfamilies, have been investigated. A preliminary screening of enzymes?performances on a large set of substrates has been carried out by a colorimetric assay performed in 96-well plates and by a pH-Stat monitoring the hydrolytic activities. Subsequently, kinetic data for selected substrates have been determined, thus elucidating the substrate preference of members of glutaryl-7-ACA acylase vs. cephalosporin C acylase subfamilies. These achievements pave the way to the ability of choosing the best enzyme for the hydrolysis of different compounds of industrial importance.