Internally consistent libraries of fluorogenic substrates demonstrate that Kex2 protease specificity is generated by multiple mechanisms

Biochemistry

Volumn 36, Issue 7, 1997, Pages 1912-1917

  Rockwell, Nathan C ^a,b   Wang, Gary T ^c   Krafft, Grant A ^d   Fuller, Robert S ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c ABBOTT LABORATORIES   (United States)

^d NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

AMINO ACID SUBSTITUTION; ARTICLE; EFFECTOR CELL; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROCESSING; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

ARGININE; BINDING, COMPETITIVE; COUMARINS; FLUORESCENT DYES; KINETICS; OLIGOPEPTIDES; PROPROTEIN CONVERTASES; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY; SUBTILISINS;

EUKARYOTA; FELIS CATUS; SACCHAROMYCES CEREVISIAE;

EID: 0031034184     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961779l     Document Type: Article

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