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    FEBS Lett. 1995 Jun 5;366(1):72-4.

    Monomeric human cathepsin E.

    Fowler SD, Kay J, Dunn BM, Tatnell PJ.

    Source

    School of Molecular and Medical Biosciences, University of Wales College of Cardiff, UK.

    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.

    PMID:
    7789521
    [PubMed - indexed for MEDLINE]

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