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Information on EC 2.1.1.98 - diphthine synthase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58456

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.98 diphthine synthase
IUBMB 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.
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Pyrococcus horikoshii
UNIPROT: O58456
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
diphthine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphthine methyltransferase
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methyltransferase, diphthine
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S-adenosyl-L-methionine:elongation factor 2 methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine-[translation elongation factor 2]-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
114514-25-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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]
show the reaction diagram
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]
show the reaction diagram
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
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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]
show the reaction diagram
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
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?
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]
show the reaction diagram
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
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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]
show the reaction diagram
the enzyme acts on His600 of elongation factor 2. It is involved in diphthamide biosynthesis
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in diphthamide biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29600
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
30000
x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 30000, SDS-PAGE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method, structure is resolved at 2.1 A resolution. The homodimeric crystal structures of the archaeal diphthine synthases from Pyrococcus horikoshii DSM 12428 and Aeropyrum pernix DSM 11879share the same overall fold as the cobalt-precorrin-4 methyltransferase CbiF
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Aeropyrum pernix (Q9YDI2), Aeropyrum pernix DSM 11879 (Q9YDI2), Pyrococcus horikoshii (O58456), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58456)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team