Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase

Homotetrameric R67 dihydrofolate reductase possesses 222 symmetry and a single active site pore. This situation results in a promiscuous binding site that accommodates either the substrate, dihydrofolate (DHF), or the cofactor, NADPH. NADPH interacts more directly with the protein as it is larger th...

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Veröffentlicht in:	Biochemistry (Easton) 2016-01, Vol.55 (1), p.133-145
Hauptverfasser:	Duff, Michael R, Chopra, Shaileja, Strader, Michael Brad, Agarwal, Pratul K, Howell, Elizabeth E
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites amines Amino Acid Sequence Binding Sites Biochemistry & Molecular Biology catalytic activity Catalytic Domain Computer Simulation crosslinking crystallography dihydrofolate reductase enzyme activity Escherichia coli - chemistry Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism folic acid Folic Acid - analogs & derivatives Folic Acid - metabolism glutamic acid Models, Molecular Molecular Sequence Data Mutagenesis Mutation NADP (coenzyme) NADP - metabolism nuclear magnetic resonance spectroscopy Oxidation-Reduction Protein Conformation Protein Multimerization Tetrahydrofolate Dehydrogenase - chemistry Tetrahydrofolate Dehydrogenase - genetics Tetrahydrofolate Dehydrogenase - metabolism
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