EC 2 - Transferases
EC 2.5 - Transferring alkyl or aryl groups, other than methyl groups
EC 2.5.1 - Transferring alkyl or aryl groups, other than methyl groups
EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 2.5.1.108
Names
Accepted name:
2-(3-amino-3-carboxypropyl)histidine synthase
Other
name:
Dph2
Systematic name:
S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase
Reaction
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36783 [IUBMB]L-histidyl-[translation elongation factor 2]GENERIC:9748Is ROOT: no
ROOT compound: GENERIC:9747Number of residues: 1S-adenosyl-L-methionineName origin: UniProt - CHECKED (C)Formula: C15H23N6O5S
Charge: 1ChEBI compound status: CHECKED (C)=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2]GENERIC:9749Is ROOT: no
ROOT compound: GENERIC:9747Number of residues: 1H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
Cofactor
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
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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]
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Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.Nature 465 : 891-896 (2010). [PMID: 20559380]
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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]