Methionine—tRNA ligase
| methionine-tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methionine--tRNA ligase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 6.1.1.10 | ||||||||
| CAS no. | 9033-22-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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 , whereas its 3 products are AMP, diphosphate, and .
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, , and .
Structural studies[]
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes 1A8H, 1F4L, 1MEA, 1MED, 1MKH, 1P7P, 1PFU, 1PFV, 1PFW, 1PFY, 1PG0, 1PG2, 1QQT, 1RQG, 1WOY, 2CSX, 2CT8, 2D54, 2D5B, 2DJV, and 2HSN.
References[]
- Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid synthetases from Escherichia coli". J. Biol. Chem. 236: 1735–1740. doi:10.1016/S0021-9258(19)63294-1.
- Lee CP, Dyson MR, Mandal N, Varshney U, Bahramian B, RajBhandary UL (1992). "Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9262–6. Bibcode:1992PNAS...89.9262L. doi:10.1073/pnas.89.19.9262. PMC 50106. PMID 1409632.
- EC 6.1.1
- Enzymes of known structure
- Ligase stubs