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Volumn 602-603, Issue , 2002, Pages 257-267

Towards understanding the origins of the different specificities of binding the reduced (NADPH) and oxidised (NADPH+) forms of nicotinamide adenine dinucleotide phosphate coenzyme to dihydrofolate reductase

(4) Polshakov, Vladimir I a,b Biekofsky, Rodolfo R a Birdsall, Berry a Feeney, James a

a NATIONAL INSTITUTE FOR MEDICAL RESEARCH (United Kingdom)

b Center for Drug Chemistry (Russian Federation)

Author keywords

Chemical shift; Density functional theory; Hydrogen bond; Lactobacillus casei dihydrofolate reductase; Nicotinamide adenine dinucleotide phosphate; Nuclear magnetic resonance

Indexed keywords

COENZYME A; DIHYDROFOLATE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BINDING AFFINITY; CIS TRANS ISOMERISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME SPECIFICITY; HYDROGEN BOND; LACTOBACILLUS CASEI; NONHUMAN; PROTEIN PROTEIN INTERACTION;

LACTOBACILLUS; LACTOBACILLUS CASEI;

EID: 0037045264 PISSN: 00222860 EISSN: None Source Type: Journal
DOI: 10.1016/S0022-2860(01)00687-1 Document Type: Article

Times cited : (13)

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