The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 98-111

  Szeltner, Zoltán ^a   Juhász, Tünde ^a   Szamosi, Ilona ^a   Rea, Dean ^b   Fülöp, Vilmos ^b   Módos, Károly ^c   Juliano, Luiz ^d   Polgár, László ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b UNIVERSITY OF WARWICK   (United Kingdom)

^c SEMMELWEIS UNIVERSITY   (Hungary)

^d FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Differential scanning calorimetry; Enzyme catalysis; Enzyme structure; Prolyl oligopeptidase; Protein engineering; X ray crystallography

Indexed keywords

PROLYL ENDOPEPTIDASE;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; KINETICS; LIGAND BINDING; MUTAGENESIS; MUTATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; TEMPERATURE;

AEROMONAS; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; MOLECULAR DYNAMICS SIMULATION; MUTATION, MISSENSE; PROTEIN STRUCTURE, SECONDARY; SERINE ENDOPEPTIDASES;

BACTERIA (MICROORGANISMS);

EID: 84869876289     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.012     Document Type: Article

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