Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. [electronic resource]
Producer: 20000711Description: 6325-35 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Aminohydrolases -- antagonists & inhibitors
- Animals
- Binding Sites
- Crystallography, X-Ray
- Drosophila
- Escherichia coli -- enzymology
- Folic Acid Antagonists -- chemistry
- Humans
- Methylenetetrahydrofolate Dehydrogenase (NADP) -- antagonists & inhibitors
- Mice
- Models, Molecular
- Molecular Sequence Data
- Multienzyme Complexes -- antagonists & inhibitors
- Mutagenesis, Site-Directed
- NADP -- metabolism
- Protein Conformation
- Rats
- Recombinant Proteins -- antagonists & inhibitors
- Sequence Alignment
- Sequence Homology, Amino Acid
- Structure-Activity Relationship
- Tetrahydrofolates -- chemistry
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Publication Type: Journal Article
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