Biology:Formylmethionine deformylase
| formylmethionine deformylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.31 | ||||||||
| CAS number | 9032-86-4 | ||||||||
| 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 formylmethionine deformylase (EC 3.5.1.31) is an enzyme that catalyzes the chemical reaction
- N-formyl-L-methionine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] formate + L-methionine
Thus, the two substrates of this enzyme are N-formyl-L-methionine and H2O, whereas its two products are formate and L-methionine.
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-methionine amidohydrolase. This enzyme participates in methionine metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1BS4, 1BS5, 1BS6, 1BS7, 1BS8, 1BSZ, 1DEF, 1DFF, 1G27, 1G2A, 1ICJ, 1JYM, 1RL4, and 2DEF.
References
- "N-Formylmethionine deformylase from Euglena gracilis". Biochem. Biophys. Res. Commun. 34 (3): 311–4. 1969. doi:10.1016/0006-291X(69)90833-X. PMID 5767026.
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