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Results 1 - 10 of 72 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more - 37338, 665767
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview 747167
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more kinetics of mutant H463F, high-pressure stopped-flow measurements, overview 726995
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more Michaelis-Menten kinetics 746778
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more Michaelis-Menten kinetics, stopped-flow kinetics, rate and equilibrium constants for pre-steady-state reaction of F464A Escherichia coli enzyme TIL with L-tryptophan 746632
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more pre-steady state kinetics and steady state kinetic study, stopped-flow measurements and stopped-flow spectra of the reaction of TIL with L-tryptophan, overview. The pH dependence of kcat/Km of Escherichia coli TIL for tryptophan exhibits 2 basic groups, with pKas of 6.0 and 7.6. The base with pKa of 7.6 is involved in the deprotonation of the alpha-carbon of substrates, and the base with pKa of 6.0 activates the indole ring of the tryptophan substrate for elimination. There is a pH-independent primary isotope effect on kcat (Dkcat = 2.5) and kcat/Km (Dkcat/Km = 2.8) for alpha-[2H]-L-tryptophan, indicating that a step (or steps) involving transfer of the alpha-proton is partially rate-limiting. The TIL reaction shows pD-independent solvent isotope effects in D2O (D2Okcat ¼ 3:8 and D2Okcat=Km ¼ 2:8), and the substrate isotope effect is reduced in D2O (Dkcat = 1.25 and Dkcat/Km = 1.82), suggesting that the steady-state solvent and substrate isotope effects are on different steps. The proton inventory for the reaction of TIL is concave downward, indicating that multiple waters are involved in the transition state of the solvent sensitive step 747245
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.1-999 - more pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, overview 727478
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.10.00181 - L-Trp - 37350
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.10.019 - indole - 37335, 37341, 37357
Show all pathways known for 4.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.10.0236 - beta-(benzimidazol-1-yl)-L-alanine mutant H463F, pH 8.0, 25°C 727478
Results 1 - 10 of 72 > >>