Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding

Journal of Biological Chemistry

Volumn 278, Issue 49, 2003, Pages 48786-48793

  Szeltneri, Zoltán ^a   Rea, Dean ^b   Renner, Veronika ^a   Juliano, Luiz ^c   Fülöp, Vilmos ^b   Polgár, László ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b UNIVERSITY OF WARWICK   (United Kingdom)

^c FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; ACYLATION; DECOMPOSITION; ENZYMES; IONIZATION; ORGANIC ACIDS; PH EFFECTS; RATE CONSTANTS; SUBSTRATES;

CHYMOTRYPSIN; ELECTROSTATIC ENVIRONMENTS; GLUTAMIC ACID; PEPTIDASES;

OLIGOMERS;

CHYMOTRYPSIN; GLUTAMIC ACID; HISTIDINE; PEPTIDASE; PROLYL ENDOPEPTIDASE; SERINE; SUBTILISIN; SERINE PROTEINASE;

ACYLATION; ARTICLE; CATALYSIS; DECOMPOSITION; ELECTRICITY; ENZYME SUBSTRATE COMPLEX; IONIZATION; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE DEPENDENCE; ANIMAL; BINDING SITE; BRAIN; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; KINETICS; METABOLISM; PH; PROTEIN BINDING; SWINE;

ARRHENIUS;

ANIMALS; BINDING SITES; BRAIN; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; SERINE ENDOPEPTIDASES; SWINE;

EID: 1542571783     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M309555200     Document Type: Article

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