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Results 1 - 10 of 154 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more - 1673
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more biphasic kinetic, linear portion near 0.5 861
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more kinetic mechanism, kinetic model 649482
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more Km-values of a number of site-specific mutant enzymes 1701
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more Km-values of mutant enzymes R30A, R30K, N74A, N74Q, and N79A 1700
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more regulation: coregulation by light of the activities of three crucial enzymes of NH4+ assimilation and transport 1704
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more steady-state kinetics 746172
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.4-999 - more the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics 716573
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.40.013 - ATP mutant E348D, glutamine-dependent activity, pH 8.0, 37°C 714228
Show all pathways known for 6.3.5.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.5.40.013 - ATP mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C 714228
Results 1 - 10 of 154 > >>