title: Stabilisation of cathepsin E by ATP.
abstract: The hydrolysis of 3 distinct substrates by cathepsin E from human red blood cells and gastric mucosa was measured in the presence and absence of physiologically relevant concentrations of ATP. At pH values below about 5.0, the nucleotide was without effect. However, at pH 5.8, whereas cathepsin E was virtually inactive by itself, it was restored to full activity (kcat) by ATP and the non-hydrolysable methylene-ATP analogue. At still higher pH values, kcat progressively diminished but significant levels of cathepsin E activity were readily detectable at pH 7.0. The specificity of this stabilisation effect was examined.
authors.affiliation: Department of Biochemistry, University College, Cardiff, Wales.
authors.forename: D J
authors.initials: DJ
authors.lastname: Thomas
authors.forename: A D
authors.initials: AD
authors.lastname: Richards
authors.forename: R A
authors.initials: RA
authors.lastname: Jupp
authors.forename: E
authors.initials: E
authors.lastname: Ueno
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: I M
authors.initials: IM
authors.lastname: Samloff
authors.forename: B M
authors.initials: BM
authors.lastname: Dunn
authors.forename: J
authors.initials: J
authors.lastname: Kay
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology*; D002384:Catalysis; D020059:Cathepsin E; D002403:Cathepsins / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D004910:Erythrocyte Membrane / Q000201:enzymology; D005753:Gastric Mucosa / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D066298:In Vitro Techniques; D010455:Peptides / Q000378:metabolism
chemical_list: D010455:Peptides; D000255:Adenosine Triphosphate; D002403:Cathepsins; D020059:Cathepsin E