Stereo-specific inhibition of sea urchin envelysin (hatching enzyme) by a synthetic autoinhibitor peptide with a cysteine-switch consensus sequence

FEBS Letters

Volumn 321, Issue 1, 1993, Pages 84-88

  Nomura, Kohji ^a   Suzuki, Norio ^b  

^a TOKYO METROPOLITAN INSTITUTE OF GERONTOLOGY   (Japan)

^b KANAZAWA UNIVERSITY   (Japan)

Author keywords

Autoinhibitor; Cysteine switch; d Cysteine; Envelysin; Hatching enzyme; Sea urchin; Stereo specificity

Indexed keywords

ENVELYSIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; ENZYME INHIBITION; NONHUMAN; PRIORITY JOURNAL; SEA URCHIN; STEREOSPECIFICITY;

AMINO ACID SEQUENCE; ANIMAL; CONSENSUS SEQUENCE; CYSTEINE; ENZYME ACTIVATION; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PEPTIDES; SEA URCHINS; STEREOISOMERISM; SUPPORT, NON-U.S. GOV'T;

EID: 0027417682     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(93)80626-6     Document Type: Article

References (20)

1. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.