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Your query returned 3 entries. Printable version
EC | 2.1.1.98 | ||||||
Accepted name: | diphthine synthase | ||||||
Reaction: | 3 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2] (overall reaction) (1a) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2] (1b) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2] (1c) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2] |
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For diagram of diphthamide biosynthesis, click here | |||||||
Glossary: | diphthine = 2-[(3S)-3-carboxy-3-(trimethylamino)propyl]-L-histidine | ||||||
Other name(s): | S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous) | ||||||
Systematic name: | S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine-[translation elongation factor 2]-forming) | ||||||
Comments: | This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine—ammonia ligase. Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). In the archaeon Pyrococcus horikoshii the enzyme acts on His600 of elongation factor 2. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 114514-25-9 | ||||||
References: |
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EC | 2.1.1.314 | ||||||
Accepted name: | diphthine methyl ester synthase | ||||||
Reaction: | 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] | ||||||
For diagram of diphthamide biosynthesis, click here | |||||||
Glossary: | diphthine methyl ester = 2-[(3S)-4-methoxy-4-oxo-3-(trimethylammonio)butyl]-L-histidine | ||||||
Other name(s): | S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous) | ||||||
Systematic name: | 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) | ||||||
Comments: | 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. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||
References: |
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EC | 3.1.1.97 | ||||||
Accepted name: | methylated diphthine methylhydrolase | ||||||
Reaction: | diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + methanol | ||||||
For diagram of diphthamide biosynthesis, click here | |||||||
Glossary: | diphthine methyl ester = 2-[(3S)-3-carboxy methyl ester-3-(trimethylammonio)propyl]-L-histidine diphthine = 2-[(3S)-3-carboxy-3-(trimethylammonio)propyl]-L-histidine |
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Other name(s): | Dph7; diphthine methylesterase (incorrect) | ||||||
Systematic name: | diphthine methyl ester acylhydrolase | ||||||
Comments: | The protein is only present in eukaryotes. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
References: |
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