Stem bromelain: Amino acid sequence and implications for weak binding of cystatin

FEBS Letters

Rawlings, Neil D.²  Buttle, David J.²  Rowan, Andrew D.²  Ritonja, Anka¹  Turk, Vito¹  Barrett, Alan J.² 

[1] Department of Biochemistry, J. Stefan Institute, Jamova 39, 61000 Ljubljana, Yugoslavia;Biochemistry Department, Strangeways Laboratory, Worts Causeway, Cambridge CB1 4RN, England

关键词: Bromelain;    Amino acid sequence;    Cysteine proteinase;    Enzyme inhibition;    Cystatin;    Compound E-64;    (Pineapple stem);    E-64;    L-3-carboxy-2;    3-trans-epoxypropionylleucylamido(4-guanidino)butane;   

DOI  :  10.1016/0014-5793(89)81383-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino acid sequence of stem bromelain, the major cysteine proteinase from pineapple stem is described. It shows that the enzyme is a member of the papain superfamily of cysteine proteinases, but is not very closely related to any other known member of this group. The sequence shows mutation or deletion of several residues that have been conserved in cysteine proteinases examined previously, including Asn-175 (papain). We suggest that some of these changes have the effect of altering the active-site geometry of stem bromelain, and that this accounts for the resistance of the enzyme to inhibition by cystatins and E-64 [L-3-carboxy-2,3-trans-epoxypropionylleucylamido(4-guanidino)butane].

【 授权许可】

Unknown