Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Zhang, Y.; Zhu, X.; Torelli, A.T.; Lee, M.; Dzikovski, B.; Koralewski, R.M.; Wang, E.; Freed, J.; Krebs, C.; Ealick, S.E.
    Lin, H.: Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme (2010), Nature, 465, 891-896.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.108 expressed in Escherichia coli Pyrococcus horikoshii
2.5.1.108 expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.108 crystal structure at 2.3 A resolution Pyrococcus horikoshii
2.5.1.108 hanging-drop vapour-diffusionmethod, X-ray crystal structure at 2.3 A resolution using selenomethionine single-wavelength anomalous diffraction phasing Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.108 Iron a [4Fe–4S] enzyme Pyrococcus horikoshii
2.5.1.108 Iron-sulfur cluster contains a [4Fe-4S] cluster, contains 1.3 and 1.9 equivalent of iron and sulfur per polypeptide Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.108 S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] Pyrococcus horikoshii
-
 S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
 ?
2.5.1.108 S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] Pyrococcus horikoshii the enzyme is involved in diphthamide biosynthesis S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.108 Pyrococcus horikoshii O58832
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.108
-
 Pyrococcus horikoshii

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.108 S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] unlike the enzymes in the radical S-adenosyl-L-methionine superfamily, Dph2 does not form the canonical 5'-deoxyadenosyl radical. Instead, it breaks the Cgamma,Met-S bond of S-adenosyl-L-methionine and generates a 3-amino-3-carboxylpropyl radical Pyrococcus horikoshii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.108 S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
-
 Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
 ?
2.5.1.108 S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] the enzyme is involved in diphthamide biosynthesis Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
-
 ?
2.5.1.108 S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
-
 Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.108 homodimer
-
 Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
2.5.1.108 physiological function the enzyme is involved in diphthamide biosynthesis Pyrococcus horikoshii