In enzymology, a N-formylmethionylaminoacyl-tRNA deformylase (EC 3.5.1.27) is an enzyme that catalyzes the chemical reaction
| N-formylmethionylaminoacyl-tRNA deformylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.27 | ||||||||
| CAS no. | 37289-08-0 | ||||||||
| 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 | ||||||||
| |||||||||
- N-formyl-L-methionylaminoacyl-tRNA + H2O formate + L-methionylaminoacyl-tRNA
Thus, the two substrates of this enzyme are N-formyl-L-methionylaminoacyl-tRNA and H2O, whereas its two products are formate and L-methionylaminoacyl-tRNA.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionylaminoacyl-tRNA amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BSJ, 1BSK, and 1LMH.
References
edit- Livingston DM, Leder P (1969). "Deformylation and protein biosynthesis". Biochemistry. 8 (1): 435–43. doi:10.1021/bi00829a059. PMID 4887858.
