Didziapetris R J, Svedas V K
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, USSR.
Biomed Biochim Acta. 1991;50(10-11):S237-42.
Kinetics of penicillin acylase-catalyzed acyl group transfer to amino acids, their esters and peptides have been analyzed. The synthesized product accumulation curves have clearly expressed a maximum. Amino acids with non-branched side chain alkyl radicals were demonstrated to be effective nucleophiles, with glycine, L-phenylalanine and L-phenylglycine being the best. D-amino acids were shown to possess much lower reactivity. Practically for all L-amino acids and peptides tested, the yield of their N-phenylacetyl derivatives in the course of penicillin acylase-catalyzed acyl group transfer reactions was found to be more than 50%. Optimization of such enzymatic synthesis required to increase its potential on the preparative scale.
对青霉素酰化酶催化的酰基转移至氨基酸、其酯类及肽类的动力学进行了分析。合成产物积累曲线呈现出明显的最大值。具有无支链侧链烷基的氨基酸被证明是有效的亲核试剂，其中甘氨酸、L-苯丙氨酸和L-苯甘氨酸效果最佳。结果表明，D-氨基酸的反应活性要低得多。实际上，对于所有测试的L-氨基酸和肽类，在青霉素酰化酶催化的酰基转移反应过程中，其N-苯乙酰基衍生物的产率均超过50%。为提高其在制备规模上的潜力，需要对这种酶促合成进行优化。
