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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.36-999 - more wild-type and mutant enzyme kinetics, caspase-1 shows positive cooperativity, a network of 21 hydrogen bonds from nine side chains connecting the active and allosteric sites change partners when going between the on-state and the off-state, an allosteric circuit promotes site-to-site coupling. Arg286 and Glu390, which form a salt bridge, have major effects, causing 100 to 200fold reductions in catalytic efficiency, kcat/Km. Two neighbors, Ser332 and Ser339, have minor effects, causing 4 to 7fold reductions, overview 699547
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.000004 - pro-interleukin-1beta pH 7.5 647635
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.0000115 - acetyl-YVAD-7-amido-4-methylcoumarin pH 7.5 647635
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.0000134 - 4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid pH 7.5 647635
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.0000215 - succinyl-YVAD-4-nitroanilide pH 7.5 647635
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.004 - acetyl-WEHD-7-amido-4-methylcoumarin pH 7.5 647424
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.006 - succinyl-YVAD-4-nitroanilide pH 7.5, 37°C 647724
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.0073 - acetyl-YEVD-4-nitroanilide pH 7.5, 30°C 647471
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.0085 - acetyl-LEVD-4-nitroanilide pH 7.5, 30°C 647471
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.360.018 - acetyl-LEVD-4-nitroanilide pH 7.5, 30°C 647471
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