The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis

Structure

Volumn 10, Issue 10, 2002, Pages 1383-1394

  Rigolet, Pascal ^a   Mechin, Ingrid ^a   Delage, Marie Madeleine ^a   Chich, Jean François ^a  

^a UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

Aminopeptidase; Peptidase family S15; PepX; Protein structure; X prolyl dipeptidyl aminopeptidase; hydrolase fold

Indexed keywords

AMINOPEPTIDASE; BACTERIAL ENZYME; HYDROLASE; MONOMER; SERINE; UNCLASSIFIED DRUG; X PROLYL DIPEPTIDYL AMINOPEPTIDASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL MEMBRANE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME SPECIFICITY; ENZYME STRUCTURE; LACTOCOCCUS LACTIS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; CATALYSIS; DIMERIZATION; DIPEPTIDYL PEPTIDASES; LACTOCOCCUS LACTIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); LACTOCOCCUS; LACTOCOCCUS LACTIS; POSIBACTERIA; STREPTOCOCCUS;

EID: 0036772305     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00851-1     Document Type: Article

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