Year: 1995
Type: article
Abstract: 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.
Source: FEBS Letters
Institutions: University of Wales, University of Florida
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: bronze
Funder: Wellcome Trust
OpenAlex ID: W1998875014