Adenylylation

AMPylator setting up target protein with ATP for AMPylation reaction.

Adenylylation,[1][2] more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino acid side chain of a protein.[3] This covalent addition of AMP to a hydroxyl side chain of the protein is a post-translational modification.[4] Adenylylation involves a phosphodiester bond between a hydroxyl group of the molecule undergoing adenylylation, and the phosphate group of the adenosine monophosphate nucleotide (i.e. adenylic acid). Enzymes that are capable of catalyzing this process are called AMPylators.

The known amino acids to be targeted in the protein are tyrosine and threonine, and sometimes serine.[5] When charges on a protein undergo a change, it affects the characteristics of the protein, normally by altering its shape via interactions of the amino acids which make up the protein. AMPylation can have various effects on the protein. These are properties of the protein like, stability, enzymatic activity, co-factor binding, and many other functional capabilities of a protein. Another function of adenylylation is amino acids activation, which is catalyzed by tRNA aminoacyl synthetase.[3] The most commonly identified protein to receive AMPylation are GTPases, and glutamine synthetase.

AMPylator having attached the ATP, now an AMP to the targeted protein, completing AMPylation.
  1. ^ Han KK, Martinage A (1992). "Post-translational chemical modification(s) of proteins". The International Journal of Biochemistry. 24 (1): 19–28. doi:10.1016/0020-711x(92)90225-p. PMID 1582530.
  2. ^ Garrett RH, Grisham CM (2007). Biochemistry (3rd ed.). Belmont, CA: Thomas. pp. 815–20.
  3. ^ a b Itzen A, Blankenfeldt W, Goody RS (April 2011). "Adenylylation: renaissance of a forgotten post-translational modification". Trends in Biochemical Sciences. 36 (4): 221–8. doi:10.1016/j.tibs.2010.12.004. PMID 21256032.
  4. ^ Woolery AR, Luong P, Broberg CA, Orth K (2010). "AMPylation: Something Old is New Again". Frontiers in Microbiology. 1: 113. doi:10.3389/fmicb.2010.00113. PMC 3095399. PMID 21607083.
  5. ^ Casey AK, Orth K (February 2018). "Enzymes Involved in AMPylation and deAMPylation". Chemical Reviews. 118 (3): 1199–1215. doi:10.1021/acs.chemrev.7b00145. PMC 5896785. PMID 28819965.