IntEnz

EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase

IntEnz Enzyme Nomenclature
EC 2.5.1.108

Names

Reaction

• 36783 [IUBMB]
  L-histidyl-[translation elongation factor 2]

  L-histidyl-[translation elongation factor 2]

  GENERIC:9748

  Is ROOT: no
  ROOT compound: GENERIC:9747

  Number of residues: 1

  L-histidine residue L-histidine residue Name origin: UniProt - CHECKED (C) CHEBI:29979 Formula: C6H7N3O Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

  +

  S-adenosyl-L-methionine

  S-adenosyl-L-methionine

  Name origin: UniProt - CHECKED (C)

  CHEBI:59789

  Formula: C15H23N6O5S
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  =

  2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2]

  2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2]

  GENERIC:9749

  Is ROOT: no
  ROOT compound: GENERIC:9747

  Number of residues: 1

  2-[(3S)-amino-3-carboxypropyl]-L-histidine residue 2-[(3S)-amino-3-carboxypropyl]-L-histidine residue Name origin: UniProt - CHECKED (C) CHEBI:73995 Formula: C10H14N4O3 Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  S-methyl-5'-thioadenosine

  S-methyl-5'-thioadenosine

  Name origin: UniProt - CHECKED (C)

  CHEBI:17509

  Formula: C11H15N5O3S
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

Cofactor

• iron-sulfur

Comments:

A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His⁷¹⁵ in mammals, His⁶⁹⁹ in yeast and His⁶⁰⁰ in Pyrococcus horikoshii. Part of diphthamide biosynthesis.

Links to other databases

References

1. Liu, S., Milne, G. T., Kuremsky, J. G., Fink, G. R., Leppla, S. H.
   Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.
   Mol. Cell. Biol. 24: 9487-9497 (2004). [PMID: 15485916]
2. 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.
   Nature 465: 891-896 (2010). [PMID: 20559380]
3. Zhu, X., Dzikovski, B., Su, X., Torelli, A. T., Zhang, Y., Ealick, S. E., Freed, J. H., Lin, H.
   Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.
   Mol Biosyst 7: 74-81 (2011). [PMID: 20931132]

[EC 2.5.1.108 created 2013]