Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
作者： M Nguyen-Distèche , M Leyh-Bouille , S Pirlot , J M Frère , J M Ghuysen
DOI: 10.1042/BJ2350167
关键词:
摘要: In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release D-lactate) and amide Ac2-L-Lys-D-Ala-D-Ala D-alanine) with accumulation acyl- (Ac2-L-Lys-D-alanyl-)enzyme. Whereas hydrolysis substrate proceeds to completion, is negligible because capacity for utilizing released D-alanine in a transfer reaction (Ac2-L-Lys-D-Ala-D-Ala + D-Ala----Ac2-L-Lys-D-Ala-D-Ala D-Ala) that maintains concentration at constant level. presence an amino acceptor X-NH2 (Gly-Gly or Gly-L-Ala) related peptidoglycan, both donors are processed without detectable acyl-enzyme. Under proper conditions, activity water and, case substrate, can be totally overcome so two substrates quantitatively converted into transpeptidated product Ac2-L-Lys-D-Ala-NH-X (and prevented). Experimental evidence suggests modifies binding enzyme ensuing rate acylation.
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