title: Monomeric human cathepsin E.
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.
authors.affiliation: School of Molecular and Medical Biosciences, University of Wales College of Cardiff, UK.
authors.forename: S D
authors.initials: SD
authors.lastname: Fowler
authors.forename: J
authors.initials: J
authors.lastname: Kay
authors.forename: B M
authors.initials: BM
authors.lastname: Dunn
authors.forename: P J
authors.initials: PJ
authors.lastname: Tatnell
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D020059:Cathepsin E; D002403:Cathepsins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002863:Chromogenic Compounds / Q000737:chemistry; D003545:Cysteine / Q000737:chemistry / Q000235:genetics; D017931:DNA Primers / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D004795:Enzyme Stability / Q000235:genetics; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002863:Chromogenic Compounds; D017931:DNA Primers; D018076:DNA, Complementary; D009842:Oligopeptides; D002403:Cathepsins; D020059:Cathepsin E; D003545:Cysteine