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Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction.
Methylenetetrahydrofolate reductases (MTHFRs; EC 126.96.36.199) catalyze the NAD(P)H-dependent reduction of 5,10-methylenetetrahydrofolate (CH(2)-H(4)folate) to 5-methyltetrahydrofolate (CH(3)-H(4)folate)… Expand
E. coli Methylenetetrahydrofolate Reductase (oxidized)
Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation.
- R. Pejchal, E. Campbell, B. Guenther, B. Lennon, R. Matthews, M. Ludwig
- Biology, Medicine
- 18 April 2006
In human methylenetetrahydrofolate reductase (MTHFR) the Ala222Val (677C-->T) polymorphism encodes a heat-labile gene product that is associated with elevated levels of homocysteine and possibly with… Expand
Comparison of functional domains in vertebrate-type ferredoxins.
The vertebrate-type Cys(4)Fe(2)S(2) ferredoxins are a class of small acidic proteins that typically act as electron shuttles between NAD(P)H-dependent reductases and monoxygenases, particularly… Expand
Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.
Putidaredoxin (Pdx), a Cys4Fe2S2 ferredoxin from Pseudomonas putida, exhibits redox-dependent binding to its physiological redox partner, cytochrome P450(cam) (CYP101), with the reduced form of Pdx… Expand
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ (Monoclinic)
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (Monoclinic)
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Methyltetrahydrofolate
Escherichia coli Methylenetetrahydrofolate Reductase (reduced) complexed with NADH, pH 7.25