Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase: Evidence for major roles in folate binding and catalysis and a minor role in flavin reactivity

Biochemistry

Volumn 44, Issue 18, 2005, Pages 6809-6822

  Trimmer, Elizabeth E ^a   Ballou, David P ^b   Galloway, Lara J ^a   Scannell, Sara A ^a   Brinker, Danielle R ^a   Casas, Katie R ^a  

^a GRINNELL COLLEGE   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; ELECTROSTATICS; ESCHERICHIA COLI; POSITIVE IONS; REDUCTION;

ELECTROSTATIC STABILIZATION; FLAVIN ADENINE DINUCLEOTIDE (FAD); METHYLENETETRAHYDROFOLATE REDUCTASE (MTHFR); MUTANT ENZYMES;

ENZYMES;

5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ALANINE; ASPARAGINE; ASPARTIC ACID; FOLIC ACID; LYSINE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SERINE; VALINE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; LOW TEMPERATURE; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; REDUCTION; STEADY STATE; WILD TYPE;

5,10-METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ALANINE; ASPARAGINE; ASPARTIC ACID; CATALYSIS; COLD; ESCHERICHIA COLI PROTEINS; FLAVIN-ADENINE DINUCLEOTIDE; FOLIC ACID; IMINES; KINETICS; LYSINE; MUTAGENESIS, SITE-DIRECTED; NAD; OXIDATION-REDUCTION; POTENTIOMETRY; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 18244368976     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0477236     Document Type: Article

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