2.4.2.17	A249T	the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme	736541	
2.4.2.17	A270D	the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme	736541	
2.4.2.17	A270P	conserved residue	721765	
2.4.2.17	C115A	the mutant shows reduced activity compared to the wild type enzyme	-, 778695	
2.4.2.17	C115S	the mutant shows 117fold reduced activity compared to the wild type enzyme	-, 778695	
2.4.2.17	D155A	slight increase in kcat, 3.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.7fold increase in Km-value for ATP	678174	
2.4.2.17	D179A	the mutant shows reduced activity compared to the wild type enzyme	-, 778695	
2.4.2.17	D179N	the mutant shows reduced activity compared to the wild type enzyme	-, 778695	
2.4.2.17	D213N	the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme	-, 736541	
2.4.2.17	E130A	site-directed mutagenesis, about 60% reduced activity compared to the wild-type enzyme, no inhibition by histidine	659495	
2.4.2.17	G230S	the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme	-, 736541	
2.4.2.17	K50A	2.3fold increase in kcat, 51fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.8fold increase in Km-value for ATP	678174	
2.4.2.17	K8A	2.5fold decrease in kcat, 4.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 3.1fold increase in Km-value for ATP	678174	
2.4.2.17	L231F/T235A	conserved residues	721765	
2.4.2.17	additional information	deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit	-, 736541	
2.4.2.17	N215K	conserved residue	721765	
2.4.2.17	N215K/L231F/T235A	conserved residues, 37fold increase in Ki-value of histidine	721765	
2.4.2.17	N215K/L231F/T235A/A270P	conserved residues	721765	
2.4.2.17	R216A	the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability	-, 758921	
2.4.2.17	R216Q	the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine	-, 758921	
2.4.2.17	R32A	the mutant shows 25fold reduced activity compared to the wild type enzyme	778695	
2.4.2.17	R56A	the mutant shows 42fold reduced activity compared to the wild type enzyme. The active site HisGS mutant shows impaired reaction chemistry which can be allosterically restored by subunit HisZ. HisZ modulates Arg32 dynamics so that it can partially compensate for the absence of Arg56	-, 778695	
2.4.2.17	R56A/K57A	the mutant shows 254fold reduced activity compared to the wild type enzyme	778695	
2.4.2.17	R70A	the mutation causes an about 5fold decrease in kcat compared to the wild type enzyme and nullifies the higher enzyme kcat with ADP as substrate observed with the wild type variant at 25°C	777101	
2.4.2.17	S140A	mutant is unstable, kinetic parameters can not be determined	678174	
2.4.2.17	S143F	the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme	-, 736541	
2.4.2.17	S232Y	the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme	736541	
2.4.2.17	S232Y/A270D	the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme	736541	
2.4.2.17	T159A	2.2fold decrease in kcat, 280fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.5fold decrease in Km-value for ATP	678174	
2.4.2.17	T162A	3.2fold decrease in kcat, 49fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.6fold decrease in Km-value for ATP	678174	
2.4.2.17	T228P	the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme	736541	
2.4.2.17	T235M	the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme	-, 736541	
2.4.2.17	Y268F/Y269F	site-directed mutagenesis, about 30% reduced activity compared to the wild-type enzyme, no inhibition by histidine	659495