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

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IntEnz Enzyme Nomenclature


Accepted name:
2-(3-amino-3-carboxypropyl)histidine synthase
Other name:
Systematic name:
S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase




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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (58) [show] [UniProt]


  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 created 2013]