Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.314
Description:Diphthine methyl ester synthase.
Alternative Name: Diphthine methyltransferase.
Cath: 3.30.950.10; 3.40.1010.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.314
BRENDA Enzyme Link: BRENDA 2.1.1.314
KEGG Enzyme Link: KEGG2.1.1.314
BioCyc Enzyme Link: BioCyc 2.1.1.314
ExPASy Enzyme Link: ExPASy2.1.1.314
EC2PDB Enzyme Link: EC2PDB 2.1.1.314
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.314
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.314
IntEnz Enzyme Link: IntEnz 2.1.1.314
MEDLINE Enzyme Link: MEDLINE 2.1.1.314
MSA:

2.1.1.314;

Phylogenetic Tree:

2.1.1.314;

Uniprot:
M-CSA:
RHEA:42652 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:8].[*:9]-[S+;H0:10](-[*:11])-[CH3;+0:12].[*:13]-[S+;H0:14](-[*:15])-[CH3;+0:16].([*:17]1:[*:18]:[n;H0;+0:19]:[*:20]:[nH;+0:21]:1.[NH2;+0:22]-[*:23]-[*:24]-[OH;+0:25])>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[S;H0;+0:6]-[*:7].[*:9]-[S;H0;+0:10]-[*:11].[*:13]-[S;H0;+0:14]-[*:15].([*:17]1:[*:18]:[nH;+0:19]:[*:20]:[n;H0;+0:21]:1.[CH3;+0:8]-[N+;H0:22](-[CH3;+0:12])(-[CH3;+0:16])-[*:23]-[*:24]-[O;H0;+0:25]-[CH3;+0:4])
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The post-translational trimethylation of diphthamide studied in vitro.Moehring JM, Moehring TJ1988 Mar 153346227
Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.Lin Z, Su X, Chen W, Ci B, Zhang S, Lin H2014 Apr 3024739148
Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase.Chen JY, Bodley JW1988 Aug 253042777
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 SH2004 Nov15485916