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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites / genetics
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Cathepsin E
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Cathepsins / chemistry*
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Cathepsins / genetics
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Cathepsins / metabolism
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Chromogenic Compounds / chemistry
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Cysteine / chemistry
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Cysteine / genetics
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DNA Primers / genetics
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DNA, Complementary / genetics
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Enzyme Stability / genetics
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Humans
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Hydrogen-Ion Concentration
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligopeptides / chemistry
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Protein Conformation
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Substrate Specificity
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Temperature
Substances
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Chromogenic Compounds
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DNA Primers
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DNA, Complementary
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Oligopeptides
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Cathepsins
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Cathepsin E
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Cysteine