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Results 1 - 10 of 95 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more - 643429, 660996, 661221
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more dissociation/association rate constants and equilibrium dissociation constants for the three dimeric enzyme forms and their nucleic acid substrates 723042
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more kinetic constants for DNA-dependent and RNA-dependent DNA polymerization Michaelis-Menten mechanism and kinetic model of the mutant enzyme, overview 723163
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more kinetics of binding of TTP and dATP to the enzyme-DNA complex, the kinetics of mismatch dATP binding are complexoverview 723783
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more Km-value for deoxynucleoside triphosphates is 0.01-0.03 mM 643418
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more Km-value for poly(rA)n*oligo(dT)12-18 is 0.004 mg/ml, Km-value for poly(rC)n*oligo(dG)12-18 is 0.0036 mg/ml, measured at pH 7.5 and 37°C 643425
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more Michaelis-Menten kinetics 721508
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more Michaelis-Menten kinetics, overview 721311
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more pre-steady state kinetic analysis of 2-deoxyadenosine 5-triphosphate compounds with wild-type and mutant K65R enzymes, overview 721815
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.49-999 - more pre-steady-state incorporation of 6-modified 3'-azido-ddGTP nucleotides by HIV-1 RT, steady-state kinetics, overview 723294
Results 1 - 10 of 95 > >>