Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase

Biochemistry

Volumn 41, Issue 25, 2002, Pages 8134-8142

  Elrod, Philip ^a,b   Zhang, Jinsong ^a   Yang, Xiaoda ^a,c   Yin, Dan ^a,d   Hu, Yongbo ^a   Borchardt, Ronald T ^a   Schowen, Richard L ^a  

^a UNIVERSITY OF KANSAS   (United States)

^b PFIZER INC   (United States)

^c PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^d MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE;

CATALYST ACTIVITY; ENZYMES; HYDROLYSIS; MUTAGENESIS; PROTONS;

BIOCHEMISTRY;

ADENOSINE; ADENOSYLHOMOCYSTEINASE; ALANINE; ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; HOMOCYSTEINE; LYSINE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; WATER;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; HUMAN; HYDROLYSIS; MICHAELIS CONSTANT; MOLECULAR STABILITY; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION TIME; REDUCTION; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS; WILD TYPE;

ADENOSYLHOMOCYSTEINASE; BINDING SITES; CATALYSIS; HUMANS; HYDROLASES; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; POINT MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 0037172784     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi025771p     Document Type: Article

References (21)