Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli ER2556 cells | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
A249T | the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
A270D | the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
D213N | the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
G230S | the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
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 | Corynebacterium glutamicum |
S143F | the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
S232Y | the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
S232Y/A270D | the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
T228P | the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
T235M | the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme | Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
beta-(2-thiazolyl)-DL-alanine | - |
Corynebacterium glutamicum | |
L-histidine | - |
Corynebacterium glutamicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Corynebacterium glutamicum | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Corynebacterium glutamicum ATCC 13032 | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | Q9Z472 | - |
- |
Corynebacterium glutamicum ATCC 13032 | Q9Z472 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Corynebacterium glutamicum | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Corynebacterium glutamicum ATCC 13032 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ATP-phosphoribosyl transferase | - |
Corynebacterium glutamicum |
HisG | - |
Corynebacterium glutamicum |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0005 | - |
L-histidine | wild type enzyme, at pH 8.5 and 30°C | Corynebacterium glutamicum | |
0.011 | - |
L-histidine | mutant enzyme A270D, at pH 8.5 and 30°C | Corynebacterium glutamicum | |
0.022 | - |
L-histidine | mutant enzyme S232Y, at pH 8.5 and 30°C | Corynebacterium glutamicum | |
0.044 | - |
L-histidine | mutant enzyme S143F, at pH 8.5 and 30°C | Corynebacterium glutamicum | |
0.178 | - |
L-histidine | mutant enzyme S232Y/A270D, at pH 8.5 and 30°C | Corynebacterium glutamicum |