Literature summary for 1.5.1.54 extracted from

Trimmer, E.E.; Ballou, D.P.; Galloway, L.J.; Scannell, S.A.; Brinker, D.R.; Casas, K.R.
Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase evidence for major roles in folate binding and catalysis and a minor role in flavin reactivity (2005), Biochemistry, 44, 6809-6822 .

Protein Variants

Protein Variants	Comment	Organism
D120A	midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased	Escherichia coli
D120K	midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased	Escherichia coli
D120N	midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased	Escherichia coli
D120S	midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased	Escherichia coli
D120V	midpoint potential of the mutant increases, the mutant exhibits a 1.2- to 1.5fold faster reduction rate than the wild-type enzyme. Catalytic efficiency (kcat/Km) in the 5-10-methylentetrahydrofolate oxidative half-reaction is significantly decreased	Escherichia coli

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEZ1	cf. EC 1.5.1.20	-