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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]
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]
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]
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]
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]
the enzyme acts on His600 of elongation factor 2. It is involved in diphthamide biosynthesis
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
the enzyme acts on His600 of elongation factor 2. It is involved in diphthamide biosynthesis
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
-
-
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
-
-
-
-
?
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]
-
-
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
the enzyme catalyzes the trimethylation in a highly processive manner. It acts on His600 of elongation factor 2. Mono- and dimethylated PhEF2 are detected, while the trimethylated product cannot be detected due to the facile elimination of the trimethylamino group
-
-
?
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]
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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]
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]
-
-
-
-
?
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]
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]
-
-
-
-
?
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]
the enzyme acts on His600 of elongation factor 2. It is involved in diphthamide biosynthesis
-
-
?
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]
the enzyme acts on His600 of elongation factor 2. It is involved in diphthamide biosynthesis
-
-
?
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
-
-
?
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]
-
-
-
-
?
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]
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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?
x * 30000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
-
dimer
2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
dimer
-
2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
-
dimer
2 * 29600, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
dimer
-
2 * 29600, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Kishishita, S.; Shimizu, K.; Murayama, K.; Terada, T.; Shirouzu, M.; Yokoyama, S.; Kunishima, N.
Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2
Acta Crystallogr. Sect. D
64
397-406
2008
Pyrococcus horikoshii (O58456), Pyrococcus horikoshii, Aeropyrum pernix (Q9YDI2), Aeropyrum pernix DSM 11879 (Q9YDI2), Pyrococcus horikoshii DSM 12428 (O58456)
brenda
Zhu, X.; Kim, J.; Su, X.; Lin, H.
Reconstitution of diphthine synthase activity in vitro
Biochemistry
49
9649-9657
2010
Pyrococcus horikoshii (O58456), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58456)
brenda
Uthman, S.; Baer, C.; Scheidt, V.; Liu, S.; ten Have, S.; Giorgini, F.; Stark, M.J.; Schaffrath, R.
The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network
PLoS Genet.
9
e1003334
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Lin, Z.; Su, X.; Chen, W.; Ci, B.; Zhang, S.; Lin, H.
Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis
J. Am. Chem. Soc.
136
6179-6182
2014
Saccharomyces cerevisiae
brenda
Hoerberg, J.; Saenz-Mendez, P.; Eriksson, L.A.
QM/MM studies of Dph5 - a promiscuous methyltransferase in the eukaryotic biosynthetic pathway of diphthamide
J. Chem. Inf. Model.
58
1406-1414
2018
Saccharomyces cerevisiae
brenda