Diphthine synthase
| diphthine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.98 | ||||||||
| CAS no. | 114514-25-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a diphthine synthase (EC 2.1.1.98) is an enzyme that catalyzes the chemical reaction
- 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
[edit]As of late 2007, 84 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1VCE, PDB: 1VHV, PDB: 1WDE, PDB: 1WNG, PDB: 2DEK, PDB: 2DSG, PDB: 2DSH, PDB: 2DSI, PDB: 2DV3, PDB: 2DV4, PDB: 2DV5, PDB: 2DV7, PDB: 2DXV, PDB: 2DXW, PDB: 2DXX, PDB: 2E07, PDB: 2E08, PDB: 2E15, PDB: 2E16, PDB: 2E17, PDB: 2E4N, PDB: 2E4R, PDB: 2E7R, PDB: 2E8H, PDB: 2E8Q, PDB: 2E8R, PDB: 2E8S, PDB: 2ED3, PDB: 2ED5, PDB: 2EEQ, PDB: 2EGB, PDB: 2EGL, PDB: 2EGS, PDB: 2EH2, PDB: 2EH4, PDB: 2EH5, PDB: 2EHC, PDB: 2EHL, PDB: 2EJJ, PDB: 2EJK, PDB: 2EJZ, PDB: 2EK2, PDB: 2EK3, PDB: 2EK4, PDB: 2EK7, PDB: 2EKA, PDB: 2EL0, PDB: 2EL1, PDB: 2EL2, PDB: 2EL3, PDB: 2ELD, PDB: 2ELE, PDB: 2EMR, PDB: 2EMU, PDB: 2EN5, PDB: 2ENI, PDB: 2HR8, PDB: 2HUQ, PDB: 2HUT, PDB: 2HUV, PDB: 2HUX, PDB: 2OWF, PDB: 2OWG, PDB: 2OWK, PDB: 2OWU, PDB: 2OWV, PDB: 2P2X, PDB: 2P5C, PDB: 2P5F, PDB: 2P6D, PDB: 2P6I, PDB: 2P6K, PDB: 2P6L, PDB: 2P9D, PDB: 2PB4, PDB: 2PB5, PDB: 2PB6, PDB: 2PCA, PDB: 2PCG, PDB: 2PCH, PDB: 2PCI, PDB: 2PCK, PDB: 2PCM, and PDB: 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.
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