Adenylation

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The adenylation (also adenylylation ) is a post-translational modification of proteins , in which an adenine group is appended.

properties

The adenylated amino acid in the protein is e.g. B. a tyrosine . Adenylation of a protein takes place by reaction of a hydroxyl group , amino group or sulfhydryl group of the protein with adenosine monophosphate , during which the phosphodiester bond is cleaved.

The extent of adenylation of glutamine synthetase depends on the ratio of glutamine to α-ketoglutarate . The larger the ratio, the more adenylation occurs in the monomers , which decreases their enzyme activity . Adenylation is therefore an indication of sufficient concentrations of glutamine-bound amine , whereas a low adenylation indicates an increased fixation of ammonia by glutamine synthetase.

The adenylating enzymes of the ANL family include e.g. B. acyl and aryl-CoA synthetases, the firefly luciferase and the adenylation domains of the modular non-ribosomal peptide synthetases (NRPS). In NRPS, adenylation initiates protein synthesis with adenosine as a leaving group .

Individual evidence

  1. ↑ KK Han, A. Martinage: Post-translational chemical modification (s) of proteins. In: The International journal of biochemistry. Volume 24, Number 1, 1992, pp. 19-28, PMID 1582530 .
  2. ^ Garrett, RH, and CM Grisham. Biochemistry. 3rd ed. Belmont, CA: Thomas, 2007. 815-820.
  3. ^ MP Müller, MF Albers, A. Itzen, C. Hedberg: Exploring adenylylation and phosphocholination as post-translational modifications. In: ChemBioChem Volume 15, Number 1, January 2014, pp. 19–26, doi : 10.1002 / cbic.201300508 . PMID 24174209 .
  4. ^ BP Duckworth, KM Nelson, CC Aldrich: Adenylating enzymes in Mycobacterium tuberculosis as drug targets. In: Current Topics in Medicinal Chemistry . Volume 12, Number 7, 2012, pp. 766-796, PMID 22283817 . PMC 3808994 (free full text).
  5. ↑ AM Gulick: Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase. In: ACS Chemical Biology . Volume 4, Number 10, October 2009, pp. 811-827, doi : 10.1021 / cb900156h . PMID 19610673 . PMC 2769252 (free full text).
  6. ^ A. Koglin, CT Walsh: Structural insights into nonribosomal peptide enzymatic assembly lines. In: Natural Product Reports . Volume 26, Number 8, August 2009, pp. 987-1000, doi : 10.1039 / b904543k . PMID 19636447 . PMC 2773127 (free full text).