Functional role of fumarate site Glu59 involved in allosteric regulation and subunit-subunit interaction of human mitochondrial NAD(P) +-dependent malic enzyme

FEBS Journal

Volumn 276, Issue 4, 2009, Pages 983-994

  Hsieh, Ju Yi ^a   Chiang, Yu Hsiu ^a   Chang, Kuan Yu ^a   Hung, Hui Chih ^a  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Allosteric regulation; Analytical ultracentrifugation; Electrostatic interaction; Malic enzyme; Mutagenesis

Indexed keywords

ASPARTIC ACID; FUMARIC ACID; GLUTAMIC ACID; GLUTAMINE; LEUCINE; MALATE DEHYDROGENASE (DECARBOXYLATING); NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME SUBUNIT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SEQUENCE ALIGNMENT; WILD TYPE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ENZYME ACTIVATION; FUMARATES; HUMANS; KINETICS; MALATE DEHYDROGENASE; MALATES; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN SUBUNITS; RECOMBINANT PROTEINS;

EID: 58849163243     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06834.x     Document Type: Article

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