A single tyrosine hydroxyl group almost entirely controls the NADPH specificity of plasmodium falciparum ferredoxin-NADP+ reductase

Biochemistry

Volumn 51, Issue 18, 2012, Pages 3819-3826

  Baroni, Sara ^a   Pandini, Vittorio ^a   Vanoni, Maria Antonietta ^a   Aliverti, Alessandro ^a  

^a UNIVERSITY OF MILAN   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL DRUG; COENZYME SPECIFICITY; COFACTOR SPECIFICITY; HYDROXYL GROUPS; KINETIC PROPERTIES; PHOSPHATE GROUP; PHOTO-REDUCTION; PLASMODIUM FALCIPARUM; SINGLE MUTATION;

AMINO ACIDS; REACTION KINETICS;

ENZYME ACTIVITY;

FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; GLUTAMINE; HISTIDINE; HYDROXYL GROUP; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TYROSINE;

ARTICLE; CATALYSIS; CHEMICAL BOND; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; MUTATION; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; REDUCTION; SPECTROPHOTOMETRY; STEADY STATE;

AMINO ACID SUBSTITUTION; BINDING SITES; COENZYMES; FERREDOXIN-NADP REDUCTASE; KINETICS; NAD; NADP; PLASMODIUM FALCIPARUM; SUBSTRATE SPECIFICITY; TYROSINE;

PLASMODIUM FALCIPARUM;

EID: 84860717536     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300078p     Document Type: Article

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