Literature summary for 2.7.7.89 extracted from

Jaggi, R.; Van Heeswijk, W.; Westerhoff, H.; Ollis, D.; Vasudevan, S.
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction (1997), EMBO J., 16, 5562-5571.

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Activating Compound

Activating Compound	Comment	Organism	Structure
2-oxoglutarate	activates the deadenylylation reaction catalysed by the N-domain	Escherichia coli
additional information	glutamine activates the adenylylation reaction of the AT-C domain, reaction of EC 2.7.7.42	Escherichia coli
uridylated signal transduction proteon PII	the deadenylylation activity of AT-N depends on PII-UMP	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	construcution of truncation mutants corresponding to amino acids 1-423 (AT-N) and 425-945 (AT-C). AT-N carries a deadenylylation activity and AT-C carries an adenylylation activity	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
signal transduction protein PII	the deadenylylation activity of AT-N is inhibited by PII	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30870	-	-

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Release 2023.1 (January 2023)