EC number:2.1.1.98
| ID: | 2.1.1.98 |
|---|---|
| Description: | Diphthine synthase. |
| Cath: | 3.30.950.10; 3.40.1010.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.98 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.98 |
| KEGG Enzyme Link: | KEGG2.1.1.98 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.98 |
| ExPASy Enzyme Link: | ExPASy2.1.1.98 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.98 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.98 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.98 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.98 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.98 |
| RHEA:36415 | 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine |
| RULE(radius=1) | ([*:1]-[NH2;+0:2].[*:3]1:[*:4]:[n;H0;+0:5]:[*:6]:[nH;+0:7]:1).[*:8]-[S+;H0:9](-[*:10])-[CH3;+0:11].[*:12]-[S+;H0:13](-[*:14])-[CH3;+0:15].[*:16]-[S+;H0:17](-[*:18])-[CH3;+0:19]>>([*:1]-[N+;H0:2](-[CH3;+0:15])(-[CH3;+0:19])-[CH3;+0:11].[*:3]1:[*:4]:[nH;+0:5]:[*:6]:[n;H0;+0:7]:1).[*:8]-[S;H0;+0:9]-[*:10].[*:12]-[S;H0;+0:13]-[*:14].[*:16]-[S;H0;+0:17]-[*:18] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The post-translational trimethylation of diphthamide studied in vitro. | Moehring JM, Moehring TJ | 1988 Mar 15 | 3346227 |
| Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase. | Chen JY, Bodley JW | 1988 Aug 25 | 3042777 |
| Reconstitution of diphthine synthase activity in vitro. | Zhu X, Kim J, Su X, Lin H | 2010 Nov 9 | 20873788 |
| Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. | Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH | 2004 Nov | 15485916 |