Monomeric human cathepsin E

FEBS Letters

Dunn, Ben M.¹  Tatnell, Peter J.²  Fowler, Sylvia D.²  Kay, John² 

[1] Department of Biochemistry and Molecular Biology, J. Hillis Miller Health Center, University of Florida, Gainesville, FL 32610, USA;School of Molecular and Medical Biosciences, University of Wales College of Cardiff, Museum Avenue, PO Box 911, Cardiff CF1 3US, UK

关键词: Human cathepsin E;    Aspartic proteinase;    Homodimer;    Mutation;    Engineered monomer;    Activity;    Stability;   

DOI  :  10.1016/0014-5793(95)00501-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cathepsin E is a homodimer, consisting of two monomers linked by an inter-molecular disulphide bond. The cysteine residue involved is located near to the N-terminus of the mature proteinase. By mutating this residue to alanine, a monomeric form of human cathepsin E was engineered and purified. The activity of the resultant enzyme was not altered significantly (in terms of its ability to hydrolyse two chromogenic peptide substrates; and its susceptibility to inhibition by pepstatin). However, the stability of the mutant enzyme to alkaline pH and to temperature was markedly reduced.

【 授权许可】

Unknown