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Results 1 - 10 of 99 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more - 36325, 36329, 36335, 36338, 36346, 36352, 586913
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more approximations for several substrates: 0.01 mM 36326
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more comparison of affinities of various substituted metalloenzymes 36340
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more comparison of Km-values in crystals and in solution 36328
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more comparison of Km-values of enzyme crystals and solution 36328
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more derivation from classical Michalis-Menten kinetics with some substrates 36322
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more dissociation constant of enzyme GlyTyr complex: 0.001, no Michaelis-Menten kinetics with some substrates, larger substrates tend to have smaller Km-values than smaller substrates 36317
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.1-999 - more Km values of immobilized enzyme generally higher than those in solution 36351
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.10.000124 - L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester - 36352
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.10.000223 - L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester - 36352
Results 1 - 10 of 99 > >>