Entry |
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Name |
2-(3-amino-3-carboxypropyl)histidine synthase;
Dph2
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Class |
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
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Sysname |
S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase
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Reaction(IUBMB) |
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] [RN: R10455]
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Reaction(KEGG) |
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Substrate |
S-adenosyl-L-methionine [CPD: C00019];
L-histidine-[translation elongation factor 2] [CPD: C20663]
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Product |
S-methyl-5'-thioadenosine [CPD: C00170];
2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] [CPD: C04441]
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Comment |
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 enzyme is a member of the 'AdoMet radical' (radical SAM) family and generates the 3-amino-3-carboxypropyl radical by an uncanonical clevage of S-adenosyl-L-methionine. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis.
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History |
EC 2.5.1.108 created 2013
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Orthology |
K07561 | 2-(3-amino-3-carboxypropyl)histidine synthase |
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Genes |
» show all
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Reference |
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Authors |
Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH |
Title |
Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. |
Journal |
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Sequence |
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Reference |
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Authors |
Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H |
Title |
Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. |
Journal |
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Sequence |
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Reference |
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Authors |
Zhu X, Dzikovski B, Su X, Torelli AT, Zhang Y, Ealick SE, Freed JH, Lin H |
Title |
Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. |
Journal |
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Sequence |
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Reference |
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Authors |
Dong M, Horitani M, Dzikovski B, Pandelia ME, Krebs C, Freed JH, Hoffman BM, Lin H |
Title |
Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme. |
Journal |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 2.5.1.108 |
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LinkDB |
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