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Literature summary for 1.5.1.3 extracted from

  • Antikainen, N.M.; Smiley, R.D.; Benkovic, S.J.; Hammes, G.G.
    Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase (2005), Biochemistry, 44, 16835-16843.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G121V reduced catalytic activity Escherichia coli
additional information double-labeling of enzyme with fluorescent quencher QSY35, at amino acid 17, and fluorescent probe Alexa555,at amino acid 35, by introducing Cys residues at these sites. Labeled enzyme retains full catalytic activity, analysis of first order rate constants for the stopped-flow fluorescent change of forward and reverse reaction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information transient kinetics investigation of enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
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