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.
^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.
^Garrett RH, Grisham CM (2007). Biochemistry (3rd ed.). Belmont, CA: Thomas. pp. 815–20.
^ abItzen 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.
^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.
^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.
Adenylylation, more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino...
residues. Adenylylation protein modification adds a negative charge to the protein and thus changes its protein function. Protein adenylylation is especially...
subunits can undergo adenylylation or deadenylylation by adenylyl transferase (AT), a bifunctional regulatory enzyme. Adenylylation is a post-translational...
activity site such as nicks in DNA segments or Okazaki fragments etc. Adenylylation (addition of AMP) of a lysine residue in the active center of the enzyme...
unit of the synthetase. Amino acids are initially adenylated by an “adenylylation” (A) domain before being attached by a thioester bond to an Acyl Carrier...
are modified by nucleotidyltransferases. The attachment of an AMP (adenylylation) or UMP (uridylylation) can activate or inactivate an enzyme or change...
protein adenylyltransferase (FICD) is an enzyme in metazoans possessing adenylylation and deadenylylation activity (also known as (de)AMPylation), and is...
phosphorylation of riboflavin into flavin mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of a C-terminal...
metal ion binding protein adenylyltransferase activity Cellular component mitochondrion Biological process protein adenylylation Sources:Amigo / QuickGO...
referred to as adenylylation, Adenosine monophosphate transfer to the DNA and Nick sealing, or phosphodiester bond formation. During adenylylation, there is...
transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin. This adenylylated ubiquitin is then transferred...
"A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response". The Journal of Biological...
Lin-Chao S, Cohen SN (July 1993). "The Escherichia coli pcnB gene promotes adenylylation of antisense RNAI of ColE1-type plasmids in vivo and degradation of...
similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This enzyme belongs to the family of transferases...
co-repressor to the glutamine synthetase by modifying it covalently (adenylylation). This modified enzyme binds to the nifR region of the nifRLA operon...
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