Differentiation of tryptic enzymes based on enantiomeric specificity at the deacylation step

FEBS Letters

Yamada, Hiroyuki¹  Kanaoka, Yuichi¹  Tanizawa, Kazutaka¹ 

[1] Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan

关键词: Trypsin;    Thrombin;    Plasmin;    Deacylation rate;    Acyl enzyme;   

DOI  :  10.1016/0014-5793(88)80897-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The chiral specificity of tryptic enzymes at their deacylation step has been determined for the first time by virtue of ‘inverse substrates’ carrying optically active acyl groups. Differentiation of tryptic enzymes was also successful with these substrates. The stability of acyl-thrombin is substantially higher than those of trypsin and plasmin when the (S)-dihydro-coumarilyl group is applied. This is in contrast to the result with its (R)-antipode in which all three enzymes are not differentiated. The use of chiral p-amidinophenyl esters is proposed as a versatile methodology for the design of specific inhibitors capable of discriminating among tryptic enzymes.

【 授权许可】

Unknown