Methionine–tRNA ligase

Methionine–tRNA ligase
Methionine–tRNA ligase monomer, Human
Identifiers
EC no.6.1.1.10
CAS no.9033-22-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a methionine–tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction

ATP + L-methionine + tRNAMet AMP + diphosphate + L-methionyl-tRNAMet

The 3 substrates of this enzyme are ATP, L-methionine, and tRNAMet, whereas its 3 products are AMP, diphosphate, and L-methionyl-tRNAMet.

This enzyme belongs to the family of ligases, to be specific those forming carbon–oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-methionine:tRNAMet ligase (AMP-forming). Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ribonucleate synthetase, methionyl-transfer RNA synthetase, methionine translase, and MetRS. This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-tRNA biosynthesis.

Role in oxidative stress

During oxidative stress, methionine–tRNA ligase might be phosphorylated, which results in promiscuity of this enzyme, where it aminoacylates methionine to various non-Met tRNAs. This in turn leads to substitution of amino acids in proteins with methionine, which helps relieve oxidative stress in the cell.[1]

Structural studies

As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1A8H​, PDB: 1F4L​, PDB: 1MEA​, PDB: 1MED​, PDB: 1MKH​, PDB: 1P7P​, PDB: 1PFU​, PDB: 1PFV​, PDB: 1PFW​, PDB: 1PFY​, PDB: 1PG0​, PDB: 1PG2​, PDB: 1QQT​, PDB: 1RQG​, PDB: 1WOY​, PDB: 2CSX​, PDB: 2CT8​, PDB: 2D54​, PDB: 2D5B​, PDB: 2DJV​, and PDB: 2HSN​.

References

  1. ↑ Aledo JC (October 2019). "Methionine in proteins: The Cinderella of the proteinogenic amino acids". Protein Science. 28 (10): 1785–1796. doi:10.1002/pro.3698. PMC 6739822. PMID 31359525.

Further reading