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Literature summary for 2.5.1.108 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
Search for more literature for 2.5.1.108

Cloned(Commentary)

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

Crystallization (Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron a [4Fe–4S] enzyme Pyrococcus horikoshii
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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]
-
 ?
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

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58832
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]
-
 ?
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]
-
 ?
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

Subunits Comment Organism
homodimer
-
 Pyrococcus horikoshii

General Information

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