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PubMed · 7789521

Monomeric human cathepsin E.

S D Fowler·J Kay·B M Dunn·P J Tatnell
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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.

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Amino Acid SequenceBase SequenceBinding SitesCathepsin ECathepsinsChromogenic CompoundsCysteineDNA PrimersDNA, ComplementaryEnzyme StabilityHumansHydrogen-Ion ConcentrationMolecular Sequence DataMutagenesis, Site-DirectedOligopeptidesProtein ConformationSubstrate SpecificityTemperatureJournal ArticleResearch Support, Non-U.S. Gov't

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S D Fowler, J Kay, B M Dunn, P J Tatnell. 1995-06-05. Monomeric human cathepsin E.. https://doi.org/10.1016/0014-5793(95)00501-y

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