1.5.1.54: methylenetetrahydrofolate reductase (NADH)
This is an abbreviated version!
For detailed information about methylenetetrahydrofolate reductase (NADH), go to the full flat file.
Reaction
Synonyms
5,10-CH2-H4folate reductase, 5,10-methylenetetrahydrofolate reductase, 5,10-methylenetetrahydrofolate reductase (FADH2), 5,10-methylenetetrahydrofolic acid reductase, 5,10-methylenetetrahydropteroylglutamate reductase, 5-methyltetrahydrofolate:(acceptor) oxidoreductase, metF, methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase, methylenetetrahydrofolate reductase, methylenetetrahydrofolic acid reductase, MSMEG_6596, MSMEG_6649, MTHFR1, MTHFR2, N5,10-methylenetetrahydrofolate reductase, N5,N10-methylenetetrahydrofolate reductase
ECTree
1.5.1.54 methylenetetrahydrofolate reductase (NADH)Advanced search results
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results (Engineering
Engineering on EC 1.5.1.54 - methylenetetrahydrofolate reductase (NADH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A177V
mutation mimicks human polymorphism A222V. Mutation does not affect kcat or the Km values but alters FAD binding
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
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
D120N
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
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
E28Q
mutant is unable to catalyze the reduction of 5,10-methylentetrahydrofolate and is inactive in the physiological oxidoreductase reaction. The mutant is able to bind methyltetrahydrofolate, but reduction of the FAD cofactor is not observed
F223A
mutation impairs NADH and 5,10-methylentetrahydrofolate binding each 40fold yet slows catalysis of both half-reactions less than 2fold
F223L
affinity for 5,10-methylentetrahydrofolate is unaffected by the mutation, the variant catalyzes the oxidative half-reaction 3fold faster than the wild-type enzyme
Q183A
in the reductive half-reaction, NADH binding affinity and the rate of flavin reduction are not hindered by the mutation. Q183A exhibits a 6-10fold lower rate of folate reduction and binds methylentetrahydrofolate with 7-fold lower affinity
Q183E
in the reductive half-reaction, NADH binding affinity and the rate of flavin reduction are not hindered by the mutation and Gln183 plays a minor in the oxidative half-reaction. The mutant displays catalytic constants within 3fold of the wild-type enzyme
additional information
chromosomal copy of MET13 is replaced by an Arabidopsis thaliana MTHFR cDNA (AtMTHFR-1) or by a chimeric sequence (Chimera-1) comprising the yeast N-terminal domain and the AtMTHFR-1 C-terminal domain. Chimera-1 uses both NADH and NADPH and is insensitive to S-adenosyl-L-methionine. Engineered yeast expressing Chimera-1 accumulates 140fold more S-adenosyl-L-methionine and 7fold more methionine than does the wild-type and grows normally. Yeast expressing AtMTHFR-1 accumulates 8fold more S-adenosyl-L-methionine
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
D120N
mutant is reduced by NADH 30% more rapidly than the wild-type enzyme
