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Information on EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase
for references in articles please use BRENDA:EC2.5.1.108
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EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.108 2-(3-amino-3-carboxypropyl)histidine synthase
IUBMB 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 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.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
- 2.5.1.108
-
diphtheria
- toxin
- horikoshii
-
pyrococcus
- s-adenosylmethionine
-
cluster-containing
- fe-s
- heterodimer
Reaction Schemes
showSynonyms
dph1-dph2, phdph2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diphthine synthase
DPH1
Dph1-Dph2
Dph2
S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
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]
The relevant histidine of translation elongation factor 2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii
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]
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-
-
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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
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PATHWAY SOURCE
PATHWAYS
MetaCyc
diphthamide biosynthesis I (archaea), diphthamide biosynthesis II (eukaryotes)
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SYSTEMATIC NAME
IUBMB Comments
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 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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5'-(3-(3-N,N-dimethylamino)phenoxy)propyl-5'-methyl-5'-thioadenosine + a protein
5'-deoxy-5'-(3-(3-N,N-dimethylamino)phenoxy)propyl-5'-thioadenosine + a methylated protein
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Substrates: -
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5'-deoxy-5'-(3-phenoxy)propyl-5'-methyl-5'-thioadenosine + a protein
5'-deoxy-5'-(3-phenoxy)propyl-5'-thioadenosine + a methylated protein
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Substrates: -
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
L-histidine-[translation elongation factor 2] + [[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl][(2E)-3-carboxyprop-2-en-1-yl]methylsulfonium
2-(3-carboxyprop-2-en-1-yl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: S-adenosyl-L-methionine analogue, in which the 3-amino-3-carboxypropyl group is replaced with a 3-carboxyallyl group. The analogue is cleaved by Dph2, yielding a paramagnetic (S = 1/2) species, which is assigned to a complex formed between the reaction product, alpha-sulfinyl-3-butenoic acid, and the [4Fe-4S] cluster. Data support a pi-complex between the C=C double bond of alpha-sulfinyl-3-butenoic acid and the unique iron of the [4Fe-4S] cluster, i.e. a radical S-adenosyl-L-methionine-related [4Fe-4S]+ cluster forming an organometallic complex with an alkene
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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]
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
Substrates: -
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
S-adenosyl-L-methionine + L-histidine699-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine699-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine715-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine715-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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additional information
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Substrates: no activity is detected using dithionite or the Dph3/Cbr1/NADH system as the reductant
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: -
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: -
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: -
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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]
Substrates: -
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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]
Substrates: -
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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]
Substrates: -
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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]
Substrates: first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2
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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]
Substrates: -
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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]
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Substrates: -
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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]
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Substrates: -
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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]
Substrates: -
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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]
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Substrates: -
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
Substrates: -
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
Substrates: the 3-amino-3-carboxypropyl radical is added to the imidazole ring in the pathway towards the formation of the product
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5'-(3-(3-N,N-dimethylamino)phenoxy)propyl-5'-methyl-5'-thioadenosine + a protein
5'-deoxy-5'-(3-(3-N,N-dimethylamino)phenoxy)propyl-5'-thioadenosine + a methylated protein
-
Substrates: -
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5'-deoxy-5'-(3-phenoxy)propyl-5'-methyl-5'-thioadenosine + a protein
5'-deoxy-5'-(3-phenoxy)propyl-5'-thioadenosine + a methylated protein
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Substrates: -
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
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]
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
Substrates: -
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine699-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine699-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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S-adenosyl-L-methionine + L-histidine715-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine715-[translation elongation factor 2]
Substrates: the enzyme is involved in diphthamide biosynthesis
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: -
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L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Substrates: -
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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]
Substrates: -
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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]
Substrates: -
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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]
Substrates: -
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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]
Substrates: first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2
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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]
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Substrates: -
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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]
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Substrates: -
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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]
Substrates: -
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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]
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Substrates: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
cleavage of a S-adenosyl-L-methionine analogue, in which the 3-amino-3-carboxypropyl group is replaced with a 3-carboxyallyl group, yields a paramagnetic (S = 1/2) species, which is assigned to a complex formed between the reaction product, alpha-sulfinyl-3-butenoic acid, and the [4Fe-4S] cluster. Data support a pi-complex between the C=C double bond of alpha-sulfinyl-3-butenoic acid and the unique iron of the [4Fe-4S] cluster, i.e. a radical S-adenosyl-L-methionine-related [4Fe-4S]+ cluster forming an organometallic complex with an alkene
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
Iron-sulfur cluster
each monomer of the dimeric enzyme contains three conserved cysteine residues that can bind a [4Fe4S] cluster. In the reduced state, the [4Fe4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule
Iron-sulfur cluster
each monomer contains three conserved cysteine residues that can bind a [4Fe-4S] cluster. In the reduced state, the [4Fe-4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule. The chemistry requires only one [4Fe-4S] cluster to be present in the Dph2 dimer although each monomer can bind a [4Fe-4S] cluster
Iron-sulfur cluster
contains a [4Fe-4S] cluster, contains 1.3 and 1.9 equivalent of iron and sulfur per polypeptide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
loss of Dph4 results in lack of diphthamide modification of eEF2 and resistance to diphtheria toxin. Dph4 mutant mice are growth retarded and have a specific digit defect with one or more additional preaxial digits
physiological function
the enzyme is involved in diphthamide biosynthesis
physiological function
the enzyme is involved in diphthamide biosynthesis
physiological function
the enzyme is involved in diphthamide biosynthesis
physiological function
first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2
physiological function
-
diphthamide biosynthesis proteins Dph1 and Dph2 interact and the first step of diphthamide formation on eukaryotic translation elongation factor eEF2 requires a complex formed in vivo between Dph1, Dph2 and Dph3
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with elongation factor 2, hanging drop vapor diffusion method, using 100 mM Tris (pH 7.2), 200 mM MgSO4, and 21% (w/v) PEG 400
hanging-drop vapour-diffusionmethod, X-ray crystal structure at 2.3 A resolution using selenomethionine single-wavelength anomalous diffraction phasing
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A114T
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
C137F
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
C341Y
the mutant of isoform DPH2 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
G113R
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
H105P
the mutant of isoform DPH2 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
H132P
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
H132R
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
H240R
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
L138P
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
S136R
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
S221P
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
Y152C
the mutant of isoform DPH1 shows reduced functionality and confers susceptibility to diphthamide deficiency syndrome
C163A
C259A/C287A
homodimeric mutant enzyme not stable. It is inactive and cannot bind a [4Fe-4S] cluster. Heterodimeric enzyme with a wild-type subunit and a mutant subunit is active
C287A
C59A
C59A/C287A
inactive mutant lacks the Fe-S cluster. A heterodimer of wild-type subunit and C59A/C287A mutant subunit is stable and active
A132T
the mutant of isoform DPH1 shows reduced functionality
C128A
-
the mutant shows reduced activity compared to the wild type enzyme
C155F
the mutant of isoform DPH1 shows reduced functionality
C362A
-
the mutant shows reduced activity compared to the wild type enzyme
C362S
the mutant of isoform DPH2 shows reduced functionality
G131R
the mutant of isoform DPH1 shows reduced functionality
H123P
the mutant of isoform DPH2 shows reduced functionality
H150P
the mutant of isoform DPH1 shows reduced functionality
H150R
the mutant of isoform DPH1 shows reduced functionality
H261A
the mutant of isoform DPH1 shows reduced functionality
L156P
the mutant of isoform DPH1 shows reduced functionality
L318S
the mutant of isoform DPH1 shows reduced functionality
L371H
the mutant of isoform DPH1 shows reduced functionality
P270R
the mutant of isoform DPH1 shows reduced functionality
P369S
the mutant of isoform DPH1 shows reduced functionality
R243P
the mutant of isoform DPH1 shows reduced functionality
R320C
the mutant of isoform DPH1 shows reduced functionality
S154R
the mutant of isoform DPH1 shows reduced functionality
S241P
the mutant of isoform DPH1 shows reduced functionality
Y168C
the mutant of isoform DPH1 shows reduced functionality
C163A
difference in the EPR spectrum of the reduced form, pronounced rhombic main features with greatly increased g-value anisotropy, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600
C163A
mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
C287A
difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600
C287A
mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
C59A
difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600
C59A
mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized nickel and benzamidine affinity column chromatography
Ni-NTA agarose resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Mus musculus (Q9CR25), Saccharomyces cerevisiae (P32461)
brenda
Zhu, X.; Dzikovski, B.; Su, X.; Torelli, A.; Zhang, Y.; Ealick, S.; Freed, J.; Lin, H.
Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis
Mol. Biosyst.
7
74-81
2011
Pyrococcus horikoshii (O58832), Pyrococcus horikoshii
brenda
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
Pyrococcus horikoshii (O58832)
brenda
Mattheakis, L.C.; Sor, F.; Collier, R.J.
Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene
Gene
132
149-154
1993
Saccharomyces cerevisiae (P32461), Saccharomyces cerevisiae FY251 (P32461)
brenda
Webb, T.R.; Cross, S.H.; McKie, L.; Edgar, R.; Vizor, L.; Harrison, J.; Peters, J.; Jackson, I.J.
Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development
J. Cell Sci.
121
3140-3145
2008
Mus musculus
brenda
Dong, M.; Horitani, M.; Dzikovski, B.; Pandelia, M.E.; Krebs, C.; Freed, J.H.; Hoffman, B.M.; Lin, H.
An organometallic complex formed by an unconventional radical SAM enzyme
J. Am. Chem. Soc.
138
9755-9758
2016
Pyrococcus horikoshii (O58832), Pyrococcus horikoshii
brenda
Abdel-Fattah, W.; Scheidt, V.; Uthman, S.; Stark, M.J.; Schaffrath, R.
Insights into diphthamide, key diphtheria toxin effector
Toxins
5
958-968
2013
Saccharomyces cerevisiae
brenda
Fenwick, M.; Dong, M.; Lin, H.; Ealick, S.
The crystal structure of Dph2 in complex with elongation factor 2 reveals the structural basis for the first step of diphthamide biosynthesis
Biochemistry
58
4343-4351
2019
Methanobrevibacter smithii (A5UMY5), Methanobrevibacter smithii DSM 861 (A5UMY5)
brenda
Dong, M.; Horitani, M.; Dzikovski, B.; Freed, J.; Ealick, S.; Hoffman, B.; Lin, H.
Substrate-dependent cleavage site selection by unconventional radical S-adenosylmethionine enzymes in diphthamide biosynthesis
J. Am. Chem. Soc.
139
5680-5683
2017
Pyrococcus horikoshii
brenda
Dong, M.; Dando, E.; Kotliar, I.; Su, X.; Dzikovski, B.; Freed, J.; Lin, H.
The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis
J. Biol. Inorg. Chem.
24
777-782
2019
Saccharomyces cerevisiae
brenda
Dong, M.; Zhang, Y.; Lin, H.
Methods for studying the radical SAM enzymes in diphthamide biosynthesis
Methods Enzymol.
606
421-438
2018
Pyrococcus horikoshii, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Uetkuer, K.; Mayer, K.; Khan, M.; Manivannan, T.; Schaffrath, R.; Brinkmann, U.
DPH1 and DPH2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models
Dis. Model. Mech.
16
dmm050207
2023
Homo sapiens (Q9BQC3), Homo sapiens (Q9BZG8), Saccharomyces cerevisiae (P32461), Saccharomyces cerevisiae (P40487)
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.108)
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