Activating Compound | Comment | Organism | Structure |
---|---|---|---|
alpha-ketoglutarate | 0.02 mM | Escherichia coli | |
glutamine | activates the adenylyltransferase reaction | Escherichia coli | |
glutamine | binding of PII signal transduction to ATase is stimulated by glutamine | Escherichia coli | |
PII signal transduction protein | activates the adenylyltransferase reaction | Escherichia coli | |
signal transduction protein PII | binding of signal transduction protein PII is stimulated by glutamine | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
cloned in Escherichia coli | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D173N/D175N | inactivation of the N-terminal nucleotidyltransferase domain by mutation of both highly conserved aspartates, mutated enzyme shows adenylyltransferase activity but lacks adenylyl-removing activity | Escherichia coli |
D463N/P467A/L469G | clustered point mutations in the central region of ATase, only 30-50% adenylyl-removing and adenylyltransferase activity of wild type enzyme, adenylyl-removing activity is inhibited by signal transduction protein PII and glutamine, adenylyltransferase activity is regulated by glutamine, signal transduction protein PII and signal transduction protein PII-UMP | Escherichia coli |
D701N/D703N | inactivation of the C-terminal nucleotidyltransferase domain by mutation of both highly conserved aspartates, mutated enzyme shows adenylyl-removing activity but lacks adenylyltransferase activity | Escherichia coli |
delata456-577 | enzyme missing amino acids 456-577 from the central region of ATase lacks adenylyl-removing activity but retains adenylyltransferase activity, adenylyltransferase activity is inhibited by signal transduction protein PII and signal transduction protein PII-UMP | Escherichia coli |
L525G/R527A/I528G | clustered point mutations in the central region of ATase, enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity, adenylyltransferase activity is strongly enhanced by glutamine | Escherichia coli |
additional information | several truncated versions of ATase are created, indicating that the N-terminal nucleotidyltransferase domain contains the adenylyl-removing active site and the C-terminal nucleotidyltransferase domain contains the adenylyltransferase active site | Escherichia coli |
additional information | truncated versions missing the C-terminal nucleotidyltransferase domain lacks both adenylyltransferase and adenylyl-removing activity, suggesting a role of the C-terminal nucleotidyltransferase domain in both activities | Escherichia coli |
additional information | truncation analysis shows that the protein contains a glutamine binding site and glutamine enhances the affinity for signal transduction protein PII | Escherichia coli |
additional information | truncation analysis shows that the protein contains multiple binding sites for signal transduction protein PII and signal transduction protein PII-UMP | Escherichia coli |
R499A/R501A/D505N/P509A/L511G | clustered point mutations in the central region of ATase, enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity, enzyme is inhibited by either signal transduction protein PII or signal transduction protein PII-UMP, adenylyltransferase activity is strongly enhanced by glutamine | Escherichia coli |
R571A/P573A/L575G | clustered point mutations in the central region of ATase, enzyme shows approx. 12.5% of adenylyl-removing activity of wild-type enzyme, adenylyl-removing activity is inhibited by glutamine and signal transduction protein PII, adenylyltransferase activity is strongly activated by glutamine | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
uridylated PII signal transduction protein | inhibits the adenylyltransferase reaction | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli | |
Mg2+ | required | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli YMC10 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
ammonium sulfate fractionation, DE-52 column chromatography, Bio-Gel A0.5M gel filtration, and phenyl Sepharose column chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl-[glutamine synthase] + phosphate | adenylyl-removing reaction | Escherichia coli | glutamine synthase + ADP | - |
r | |
adenylyl-[glutamine synthase] + phosphate | adenylyl-removing reaction | Escherichia coli YMC10 | glutamine synthase + ADP | - |
r | |
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | - |
Escherichia coli | diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP) | - |
? | |
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | - |
Escherichia coli YMC10 | diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP) | - |
? | |
glutamine synthase + ATP | adenylyltransferase reaction | Escherichia coli | adenylyl-[glutamine synthase] + diphosphate | - |
r | |
glutamine synthase + ATP | adenylyltransferase reaction | Escherichia coli YMC10 | adenylyl-[glutamine synthase] + diphosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
ATASE | - |
Escherichia coli |
glutamine synthetase adenylyltransferase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |