N-formylmethionylaminoacyl-tRNA deformylase
Appearance
N-formylmethionylaminoacyl-tRNA deformylase | |||||||||
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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 | ||||||||
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In enzymology, a N-formylmethionylaminoacyl-tRNA deformylase (EC 3.5.1.27) is an enzyme that catalyzes the chemical reaction
- 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
[edit]As 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.