Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain: The effects of site-directed mutagenesis of NADP binding residues

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1479, Issue 1-2, 2000, Pages 59-68

  Pawelek, Peter D ^a   Allaire, Marc ^b   Cygler, Miroslaw ^b,c   MacKenzie, Robert E ^a,c  

^a MCGILL UNIVERSITY   (Canada)

^b NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^c Montreal Jt Ctr for Struct Biol   (Canada)

Author keywords

2' Phosphate binding; Methylenetetrahydrofolate dehydrogenase cyclohydrolase; Site directed mutagenesis; Substrate channeling

Indexed keywords

METHYLENETETRAHYDROFOLATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID COMPOSITION; ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY;

AMINOHYDROLASES; BINDING SITES; HUMANS; METHYLENETETRAHYDROFOLATE DEHYDROGENASE (NADP); MODELS, MOLECULAR; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; NADP; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

STAPHYLOCOCCUS PHAGE 3A;

EID: 0034659692     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00058-3     Document Type: Article

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