| Entry |
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| Name |
diphthine methyl ester synthase;
S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous);
diphthine methyltransferase (ambiguous);
Dph5 (ambiguous)
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| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
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| Sysname |
S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine methyl ester-[translation elongation factor 2]-forming)
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| Reaction(IUBMB) |
4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 4 S-adenosyl-L-homocysteine + diphthine methyl ester-[translation elongation factor 2] [RN: R11165]
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| Reaction(KEGG) |
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| Substrate |
S-adenosyl-L-methionine [CPD: C00019];
2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] [CPD: C04441]
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| Product |
S-adenosyl-L-homocysteine [CPD: C00021];
diphthine methyl ester-[translation elongation factor 2] [CPD: C21151]
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| Comment |
This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known.
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| History |
EC 2.1.1.314 created 2015
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| Orthology |
| K00586 | diphthine methyl ester synthase |
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| Genes |
» show all
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| Reference |
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| Authors |
Chen JY, Bodley JW. |
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| Title |
Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase. |
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| Journal |
J Biol Chem 263:11692-6 (1988) |
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| Reference |
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| Authors |
Moehring JM, Moehring TJ. |
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| Title |
The post-translational trimethylation of diphthamide studied in vitro. |
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| Journal |
J Biol Chem 263:3840-4 (1988) |
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| Reference |
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| Authors |
Lin Z, Su X, Chen W, Ci B, Zhang S, Lin H |
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| Title |
Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.1.1.314 |
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