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Literature summary for 1.5.1.20 extracted from
- Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction (2005), Biochemistry, 44, 11447-11457.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| His-tagged wild-type and mutant E28Q | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E28Q | crystallization data | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ | NADH adopts a hairpin conformation and is sandwiched between a conserved phenylalanine, F223, and the isoalloxazine ring of FAD, resulting in a complex competent for hydride transfer. The binding sites of the two substrates overlap. Pinog-pong reaction is facilitated by motions of loops L2, L3, L4 | Escherichia coli |
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