EC Number   |
Activating Compound |
Reference |
|---|
  2.7.7.89 | 2-oxoglutarate |
activates the deadenylylation reaction catalysed by the N-domain |
733719 |
| 2.7.7.89 | 2-oxoglutarate |
activation |
81112 |
| 2.7.7.89 | 2-oxoglutarate |
controls the extent of activation or inhibition of the enzyme by PII or PII-UMP. 2-oxoglutarate acts exclusively through its binding to PII and PII-UMP, and does not alter the binding of PII or PII-UMP to the enzyme |
672243 |
| 2.7.7.89 | adenosine |
activation by nucleotides, most efficient in presence of two different nucleotides |
81112 |
| 2.7.7.89 | GTP |
activation by nucleotides, most efficient in presence of two different nucleotides |
81112 |
| 2.7.7.89 | ITP |
activation by nucleotides, most efficient in presence of two different nucleotides |
81112 |
| 2.7.7.89 | more |
glutamine activates the adenylylation reaction of the AT-C domain, reaction of EC 2.7.7.42 |
733719 |
| 2.7.7.89 | signal transduction protein PII |
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain |
702300 |
| 2.7.7.89 | UMP |
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain |
702300 |
| 2.7.7.89 | uridylated signal transduction protein PII |
the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by PII. The adenylyltransferase reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The enzyme appears to contain two distinct sites for PII and PII-UMP. The PII, PII-UMP, and glutamine sites are in communication. The binding of PII is favored by glutamine and its level reduced by PII-UMP, whereas glutamine and PII-UMP compete for the enzyme |
672243 |
