3.5.1.84	C175S	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	
3.5.1.84	F41A	kcat/Km for buiret is 540fold lower than the wild-type value	746233	
3.5.1.84	F41L	kcat/Km for buiret is 713fold lower than the wild-type value	746233	
3.5.1.84	F41W	kcat/Km for buiret is 73fold lower than the wild-type value	746233	
3.5.1.84	F41Y	kcat/Km for buiret is 139fold lower than the wild-type value	746233	
3.5.1.84	K142A	kcat/Km for buiret is 297fold lower than the wild-type value	746233	
3.5.1.84	Q215A	kcat/Km for buiret is 419fold lower than the wild-type value	746233	
3.5.1.84	Q215E	kcat/Km for buiret is 1302fold lower than the wild-type value	746233	
3.5.1.84	Q215N	kcat/Km for buiret is 38fold lower than the wild-type value	746233