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Literature summary for 1.5.1.3 extracted from

  • Venkitakrishnan, R.P.; Zaborowski, E.; McElheny, D.; Benkovic, S.J.; Dyson, H.J.; Wright, P.E.
    Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle (2004), Biochemistry, 43, 16046-16055.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G121V the mutation interferes with coupled loop movements and appears to impair catalysis by destabilizing the closed Michaelis complex and introducing an extra step into the kinetic pathway Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
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