Structure and function of an isozyme of earthworm proteases as a new biocatalyst

Manabu Sugimoto, Kohji Ishihara, Nobuyoshi Nakajima

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    The amino acid sequence of the earthworm-serine protease, isozyme C, which shows not only elastase-like activity but also trypsin-like activity, was determined. The catalytic triad of the trypsin family, His, Asp, Ser, was conserved in isozyme C, but the primary substrate determinant of trypsin, Asp, was missing in isozyme C, the same as in elastase. One of the two Gly at the entrance of the substrate-binding pocket of trypsin was replaced by Val as in elastase, however, the other was replaced by Ser whereas Thr is present in elastase. Furthermore, isozyme C also showed esterase-like activity, which was applicable for the synthesis of useful substances.

    Original languageEnglish
    Pages (from-to)405-409
    Number of pages5
    JournalJournal of Molecular Catalysis B: Enzymatic
    Volume23
    Issue number2-6
    DOIs
    Publication statusPublished - Sep 1 2003

    Keywords

    • Earthworm
    • Elastase
    • Esterase-like activity
    • Serine protease

    ASJC Scopus subject areas

    • Catalysis
    • Bioengineering
    • Biochemistry
    • Process Chemistry and Technology

    Fingerprint

    Dive into the research topics of 'Structure and function of an isozyme of earthworm proteases as a new biocatalyst'. Together they form a unique fingerprint.

    Cite this