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PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation

The Journal of Biological Chemistry

Feb 21, 2003

Dilip ChanduDipankar Nandi

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Abstract

Succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin (Suc-LLVY-AMC), a fluorogenic endopeptidase substrate, is used to detect 20 S proteasomal activity from Archaea to mammals. An o-phenanthroline-sensitive Suc-LLVY-AMC hydrolyzing activity was detected in Escherichia coli although it lack...read more

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Multicatalytic endopeptidase complex
Cleaved Cell
Enzymes, antithrombotic
Proteolytic Enzyme
Enzymes, peripheral vasodilators
Homologous Sequences, Amino Acid
Mycobacterium Infections
Mycobacterium smegmatis
Homologous Gene
Mutant
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  • PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation

    The Journal of Biological Chemistry

    Feb 21, 2003

    Dilip ChanduDipankar Nandi

    PMID: 12482750

    DOI: 10.1074/jbc.m207926200

    Abstract

    Succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin (Suc-LLVY-AMC), a fluorogenic endopeptidase substrate, is used to detect 20 S proteasomal activity from Archaea to mammals. An o-phenanthroline-sensitive Suc-LLVY-AMC hydrolyzing activity was detected in Escherichia coli although it lack...read more

    Mentioned in this Paper

    Multicatalytic endopeptidase complex
    Cleaved Cell
    Enzymes, antithrombotic
    Proteolytic Enzyme
    Enzymes, peripheral vasodilators

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