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Literature summary for 1.5.1.3 extracted from

  • Chopra, S.; Dooling, R.M.; Horner, C.G.; Howell, E.E.
    A balancing act between net uptake of water during dihydrofolate binding and net release of water upon NADPH binding in R67 dihydrofolate reductase (2008), J. Biol. Chem., 283, 4690-4698.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
I68M compared to wild-type, low kcat/Km (DHF) values. Mutant allows growth in presence of sorbitol up to 1.44 osmol conditions Escherichia coli
Q67H mutant with reasonable catalytic efficiency, but displays substrate and cofactor inhibition. Contrary to wild-type which allows growth on all sorbitol conditions until the osmolyte concentration becomes too high or cell water content becomes too low, mutant Q67H allows growth up to 1.81 osmol conditions Escherichia coli
Y69L compared to wild-type, low kcat/Km (DHF) values. Mutant allows growth in presence of sorbitol up to 0.81 osmol conditions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00383 plasmid-encoded isoform R67
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Reaction

Reaction Comment Organism Reaction ID
5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ binding of NADPH is accompanied by release of 38 water molecules, while binding of dihydrofolate is accompanied by the net uptake of water Escherichia coli