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FEBS Letters

Volumn 506, Issue 3, 2001, Pages 201-206

Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain

(6) Olsen, Johan Gotthardt a Kadziola, Anders a Lauritzen, Conni b Pedersen, John b Larsen, Sine a Dahl, Soren Weis b

a UNIVERSITY OF COPENHAGEN (Denmark)

b Prozymex A/S (Denmark)

Author keywords

Aminopeptidase; Cathepsin C; Chloride binding; Papain fold; Subunit interaction; Zymogen activation

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; CHLORIDE ION; DIPEPTIDYL PEPTIDASE I; PAPAIN; PROTEIN SUBUNIT; TETRAMER;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBUNIT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; STRUCTURE ANALYSIS;

ANIMALS; DIPEPTIDYL PEPTIDASE I; MODELS, MOLECULAR; PROTEIN CONFORMATION; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0035850917 PISSN: 00145793 EISSN: None Source Type: Journal
DOI: 10.1016/S0014-5793(01)02911-8 Document Type: Article

Times cited : (31)

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