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Results 1 - 10 of 124 > >>
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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.2-999 - more Michaelis–Menten model 737771
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.2-999 - more R297A mutant protein: increased apparent KM-values for ATP and FMN by about 5 and 3times, respectively, compared to the wild-type enzyme 705146
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.2-999 - more steady-state kinetic analysis of wild-type and mutant enzymes. The enzyme from Candida glabrata apparently binds its substrates with high affinity, but the overall turnover rate is very slow due to product inhibition 737678
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.00013 - FMN pH 7.5, 37°C 761953
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.00035 - FMN at 37°C, in 50 mM Tris-HCl, pH 7.5 722239
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.00036 - FMN - 705590
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.00036 - FMN at 37°C 676979
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.00038 - FMN pH 7.0, 25°C, recombinant mutant R66E 737771
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.0004 - FAD pH 7.6, 25°C 643003
Show all pathways known for 2.7.7.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.20.0004 - FMN 37°C 676979
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