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Literature summary for 1.5.1.54 extracted from

  • Lee, M.N.; Takawira, D.; Nikolova, A.P.; Ballou, D.P.; Furtado, V.C.; Phung, N.L.; Still, B.R.; Thorstad, M.K.; Tanner, J.J.; Trimmer, E.E.
    Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli (2009), Biochemistry, 48, 7673-7685 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structures of ligand-free mutants F223L and F223L/E28Q in complex with 5,10-methylentetrahydrofolate, at 1.65 and 1.70 A resolution, respectively. The folate is bound in a catalytically competent conformation, and residue Leu223 undergoes a conformational change similar to that observed for Phe223 in the E28Q-5,10-methylentetrahydrofolate structure Escherichia coli

Protein Variants

Protein Variants Comment Organism
F223A mutation impairs NADH and 5,10-methylentetrahydrofolate binding each 40fold yet slows catalysis of both half-reactions less than 2fold Escherichia coli
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 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEZ1 cf. EC 1.5.1.20
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