Characterization of Helicobacter pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis

Biochemistry

Volumn 46, Issue 46, 2007, Pages 13407-13414

  Morrow, Amy L ^a   Williams, Kristin ^a   Sand, Aaron ^a   Boanca, Gina ^a   Barycki, Joseph J ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BIOMOLECULES; CATALYST ACTIVITY; HYDROGEN BONDS; HYDROLYSIS;

HELICOBACTER PYLORI Γ-GLUTAMYLTRANSPEPTIDASE (HPGT); INTRAMOLECULAR AUTOCATALYTIC CLEAVAGE; N-TERMINAL NUCLEOPHILE HYDROLASE SUPERFAMILY;

PROTEINS;

GAMMA GLUTAMYLTRANSFERASE; GLUTAMIC ACID; HETERODIMER; POLYPEPTIDE; TYROSINE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME SPECIFICITY; HELICOBACTER PYLORI; HYDROGEN BOND; HYDROLYSIS; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN EXPRESSION;

BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; GAMMA-GLUTAMYLTRANSFERASE; GLUTAMIC ACID; HELICOBACTER PYLORI; HYDROLYSIS; KINETICS; LIGANDS; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TYROSINE;

HELICOBACTER PYLORI;

EID: 36248940234     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701599e     Document Type: Article

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