show all | hide all No of entries

Information on EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase and Organism(s) Mus musculus and UniProt Accession Q9CR25

for references in articles please use BRENDA:EC2.5.1.108
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Mus musculus
UNIPROT: Q9CR25
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The taxonomic range for the selected organisms is: Mus musculus
Synonyms
diphthine synthase, Dph2, DPH4, PhDph2, S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dph2
298647
-
DPH4
244
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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]
show the reaction diagram
The relevant histidine of translation elongation factor 2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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]
show the reaction diagram
the enzyme is involved in diphthamide biosynthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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]
show the reaction diagram
Q9CR25
the enzyme is involved in diphthamide biosynthesis
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
required for diphthamide biosynthesis; the enzyme is involved in diphthamide biosynthesis
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
DPH2_MOUSE
489
0
52365
Swiss-Prot
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and in NIH-3T3 cells
-
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Select items on the left to see more content.