In enzymology, a diphthine synthase (EC 2.1.1.98) is an enzyme that catalyzes the chemical reaction
| diphthine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.98 | ||||||||
| CAS no. | 114514-25-9 | ||||||||
| 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 | ||||||||
| |||||||||
- S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-(3-carboxy-3-aminopropyl)-L-histidine, whereas its two products are S-adenosylhomocysteine and [[2-[3-carboxy-3-(methylammonio)propyl]-L-histidine]].
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine methyltransferase. Other names in common use include S-adenosyl-L-methionine:elongation factor 2 methyltransferase, and diphthine methyltransferase.
Structural studies
editAs of late 2007, 84 structures have been solved for this class of enzymes, with PDB accession codes 1VCE, 1VHV, 1WDE, 1WNG, 2DEK, 2DSG, 2DSH, 2DSI, 2DV3, 2DV4, 2DV5, 2DV7, 2DXV, 2DXW, 2DXX, 2E07, 2E08, 2E15, 2E16, 2E17, 2E4N, 2E4R, 2E7R, 2E8H, 2E8Q, 2E8R, 2E8S, 2ED3, 2ED5, 2EEQ, 2EGB, 2EGL, 2EGS, 2EH2, 2EH4, 2EH5, 2EHC, 2EHL, 2EJJ, 2EJK, 2EJZ, 2EK2, 2EK3, 2EK4, 2EK7, 2EKA, 2EL0, 2EL1, 2EL2, 2EL3, 2ELD, 2ELE, 2EMR, 2EMU, 2EN5, 2ENI, 2HR8, 2HUQ, 2HUT, 2HUV, 2HUX, 2OWF, 2OWG, 2OWK, 2OWU, 2OWV, 2P2X, 2P5C, 2P5F, 2P6D, 2P6I, 2P6K, 2P6L, 2P9D, 2PB4, 2PB5, 2PB6, 2PCA, 2PCG, 2PCH, 2PCI, 2PCK, 2PCM, and 2Z6R.
References
edit- Chen JY, Bodley JW (1988). "Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase". J. Biol. Chem. 263 (24): 11692–6. doi:10.1016/S0021-9258(18)37839-6. PMID 3042777.
- Moehring JM, Moehring TJ (1988). "The post-translational trimethylation of diphthamide studied in vitro". J. Biol. Chem. 263 (8): 3840–4. doi:10.1016/S0021-9258(18)69001-5. PMID 3346227.
