Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

被引:1
|
作者
Morozova, I. A. [1 ]
Guranda, D. T. [1 ]
Panin, N., V [1 ,2 ]
Svedas, V. K. [1 ,2 ,3 ]
机构
[1] Lomonosov Moscow State Univ, Belozersky Inst Physicochem Biol, Moscow 119234, Russia
[2] Lomonosov Moscow State Univ, Res Comp Ctr, Moscow 119234, Russia
[3] Lomonosov Moscow State Univ, Fac Bioengn & Bioinformat, Moscow 119234, Russia
来源
ACTA NATURAE | 2023年 / 15卷 / 01期
基金
俄罗斯科学基金会;
关键词
penicillin acylases; substrate specificity; enzymatic deprotection of functional groups; N-benzyloxycarbonyl derivatives of amino acids; ESCHERICHIA-COLI; ENZYME; REMOVAL;
D O I
10.32607/actanaturae.13703
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Changes in the structure of the N-acyl group in N-acylated amino acid derivatives significantly affect both the recognition and activity of penicillin acylases on this series of substrates. However, penicillin acylases from both Alcaligenes faecalis and Escherichia coli are capable of removing the N-benzyloxycarbonyl protecting group in amino acid derivatives under mild conditions without the use of toxic reagents. Efficiency in using penicillin acylases in preparative organic synthesis can be improved by utilizing modern rational enzyme design methods.
引用
收藏
页码:69 / 73
页数:5
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