Subunit III of ruminant procarboxypeptidase A‐S6 complexes and pancreatic proteases E a new family of pancreatic serine endopeptidases?

FEBS Letters

Chapus, Catherine¹  Cambillau, Christian³  Kerfelec, Brigitte¹  Sciaky, Martine² 

[1] Centre de Biochimie et de Biologie Moléculaire du CNRS, Boîte postale 71, F-13402 Marseille Cedex 9, France;Centre de Résonnance Magnétique Biologique et Médicale, Faculté de Médecine, 27 boulevard Jean Moulin, 13005 Marseille, France;Groupe de Cristallographie des Protéines, CRMC2-CNRS, Campus de Luminy, case 913, Marseille Cedex 9, France

关键词: Serine protease;    Inactive protease;    Protease E;    (Pancreas).;    PCPA-S6;    procarboxypeptidase A-S6 ternary complex;    BSIII;    bovine subunit III;    HPE;    human protease E;    PE1;    porcine elastase 1;    TFAI;    trifluoroacetyl-L-lysyl-L-alanyl p-trifluoromethylphenylanilide;   

DOI  :  10.1016/0014-5793(88)80392-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subunit III (BSIII) of the bovine ternary complex of procarboxypeptidase A-S6 (PCPA-S6), a defective serine endopeptidase-like protein, actively synthesized by the pancreas of some ruminant species, is highly homologous to human protease E (HPE). Both proteins possess the same atypical disulfide bridge in position 98–99b. They are structurally related to porcine elastase 1 and human elastase 2 (about 56% identity). However, in contrast to those two enzymes which have an overall positive net charge, BSIII and HPE are negatively charged. Three-dimensional models of BSIII and HPE have been constructed from the crystallographic structure of porcine pancreatic elastase 1. The inhibitor-binding site for TFAI in these three proteins seems to be very similar; the atypical disulfide bridge does not seem to be involved in this binding site. The specific structural features of BSIII and HPE strongly support the assumption that BSIII is a truncated protease E and that both proteins belong to a separate serine endopeptidase family.

【 授权许可】

Unknown