Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C

Amino Acids

Volumn 46, Issue 4, 2014, Pages 931-943

  Poreba, Marcin ^a   Mihelic, Marko ^b   Krai, Priscilla ^c   Rajkovic, Jelena ^b   Krezel, Artur ^d   Pawelczak, Malgorzata ^e   Klemba, Michael ^c   Turk, Dusan ^b   Turk, Boris ^b   Latajka, Rafal ^a   Drag, Marcin ^a  

^a WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

^b JO EF STEFAN INSTITUTE   (Slovenia)

^c VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^d UNIVERSITY OF WROC AW   (Poland)

^e UNIVERSITY OF OPOLE   (Poland)

Author keywords

Cysteine protease; Fluorogenic substrate; Non proteinogenic; Substrate library; Unnatural amino acid

Indexed keywords

AMINO ACID; DIPEPTIDE; DIPEPTIDYL PEPTIDASE I; PROTOZOAL PROTEIN;

ANIMAL; BOVINE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME SPECIFICITY; ENZYMOLOGY; HUMAN; KINETICS; METABOLISM; PLASMODIUM FALCIPARUM; SYNTHESIS;

AMINO ACIDS; ANIMALS; CATHEPSIN C; CATTLE; DIPEPTIDES; HUMANS; KINETICS; MOLECULAR STRUCTURE; PLASMODIUM FALCIPARUM; PROTOZOAN PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84898847471     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-013-1654-2     Document Type: Article

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