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Results 1 - 9 of 9
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84C175S the mutant enzyme binds biuret but is non-catalytic. The structure of the inactive C175S mutant enzyme with substrate bound in the active site reveals that an active site cysteine (Cys175), aspartic acid (Asp36) and lysine (Lys142) form a catalytic triad, which is consistent with biochemical studies of enzyme variants 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84F41A kcat/Km for buiret is 540fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84F41L kcat/Km for buiret is 713fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84F41W kcat/Km for buiret is 73fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84F41Y kcat/Km for buiret is 139fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84K142A kcat/Km for buiret is 297fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84Q215A kcat/Km for buiret is 419fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84Q215E kcat/Km for buiret is 1302fold lower than the wild-type value 746233
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.84Q215N kcat/Km for buiret is 38fold lower than the wild-type value 746233
Results 1 - 9 of 9