A100L |
site-directed mutagenesis, inactive mutant |
Escherichia coli |
A13K |
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme |
Escherichia coli |
A13R |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
A30L |
site-directed mutagenesis, the mutant shows 93% reduced activity compared to the wild-type enzyme |
Escherichia coli |
D80A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
D80E |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
D80N |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
D81A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
D81K |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
D95A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
D95E |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
D95N |
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme |
Escherichia coli |
E28A |
site-directed mutagenesis, the mutation principally affects the binding of the Zn2+ ion, In the absence of the E28 side chain the zinc ions become purely coordinated by E76 and the ATP phosphates, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
E28D |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
E28N |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
E28Q |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
E28R |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
E34A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
E34D |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
E34Q |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
E69A |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
E69D |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
E69Q |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
E76A |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
E76A |
site-directed mutagenesis, the mutation principally affects the binding of the Zn2+ ion |
Escherichia coli |
E76D |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
E76Q |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
G20A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
G83P |
site-directed mutagenesis, inactive mutant |
Escherichia coli |
G97P |
site-directed mutagenesis, inactive mutant |
Escherichia coli |
K94A |
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, almost inactive mutant |
Escherichia coli |
K94M |
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
K94R |
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, almost inactive mutant |
Escherichia coli |
N72A |
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 |
Escherichia coli |
N72D |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
N72Q |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
R32A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
R32K |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
R9A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
R9E |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
R9H |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
R9K |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
Escherichia coli |
S17A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
S73A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
Escherichia coli |
S90P |
site-directed mutagenesis, inactive mutant |
Escherichia coli |
S98A |
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme |
Escherichia coli |
Y86A |
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme |
Escherichia coli |
Y86F |
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme |
Escherichia coli |