A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme

Biochemistry

Volumn 44, Issue 9, 2005, Pages 3626-3635

  Karsten, William E ^a   Liu, Dali ^a   Rao, G S Jagannatha ^b   Harris, Ben G ^b   Cook, Paul F ^a  

^a UNIVERSITY OF OKLAHOMA   (United States)

^b UNIVERSITY OF NORTH TEXAS HEALTH SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL REACTIONS; CONFORMATIONS; MUTAGENESIS; PARAMETER ESTIMATION; PH EFFECTS;

ACTIVE SITES; ACTIVITY LOSS; KINETIC PARAMETERS; RESIDUES;

ENZYMES;

MALATE DEHYDROGENASE;

ACID BASE BALANCE; AMINO ACID SEQUENCE; ARTICLE; ASCARIS SUUM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; HYDROGEN BOND; MUTATIONAL ANALYSIS; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; ARGININE; ASCARIS SUUM; ASPARTIC ACID; CATALYTIC DOMAIN; DEUTERIUM EXCHANGE MEASUREMENT; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MALATE DEHYDROGENASE; MODELS, CHEMICAL; NAD; PHENYLALANINE; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 14644404936     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047826o     Document Type: Article

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