Human cathepsin H: Deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase

Biological Chemistry

Volumn 384, Issue 9, 2003, Pages 1327-1332

  Dodt, Johannes ^a,b   Reichwein, Jörg ^a  

^a DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

^b PAUL EHRLICH INSTITUT   (Germany)

Author keywords

Cysteine protease inhibitors; Cysteine proteases; Recombinant cathepsin H; Specificity

Indexed keywords

AMINO ACID; AMINOPEPTIDASE; CATHEPSIN H; CYSTATIN; EGG WHITE; ENZYME INHIBITOR; GLUTAMIC ACID; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PROTEINASE; THREONINE;

ARTICLE; CHICKEN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE DELETION; GENE MUTATION; GENETIC ENGINEERING; HUMAN; HYDROLYSIS KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; REGULATOR GENE; STRUCTURE ACTIVITY RELATION;

AMINOPEPTIDASES; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; ENDOPEPTIDASES; ENZYME INHIBITORS; HUMANS; KINETICS; PROTEIN ENGINEERING; SEQUENCE DELETION; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

GALLUS GALLUS;

EID: 0141857294     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.149     Document Type: Article

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