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BRENDA support

Literature summary for 2.7.7.42 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
glutamine activates the adenylylation reaction of the AT-C domain Escherichia coli
signal transduction protein PII the adenylylation activity of AT-C is independent of PII (or PII-UMP), whereas in the intact enzyme PII is required for this activity 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, reaction of EC 2.7.7.89, and AT-C carries an adenylylation activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P30870
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