KEGG   ENZYME: 2.4.2.36Help
Entry
EC 2.4.2.36                 Enzyme                                 

Name
NAD+---diphthamide ADP-ribosyltransferase;
ADP-ribosyltransferase;
mono(ADPribosyl)transferase;
NAD---diphthamide ADP-ribosyltransferase;
NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase
Class
Transferases;
Glycosyltransferases;
Pentosyltransferases
BRITE hierarchy
Sysname
NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase
Reaction(IUBMB)
NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] [RN:R04074]
Reaction(KEGG)
Substrate
NAD+ [CPD:C00003];
diphthamide-[translation elongation factor 2]
Product
nicotinamide [CPD:C00153];
N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Comment
Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+---protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.
History
EC 2.4.2.36 created 1990, modified 2013
Orthology
K00776  NAD-diphthamide ADP-ribosyltransferase
K10928  cholera enterotoxin subunit A
Genes
ECW: EcE24377A_F0020(eltA)
ELH: ETEC_p666_0660(eltA)
EUN: UMNK88_pEnt35(eltA)
VCH: VC1457
VCF: IR04_12525
VCS: MS6_1231 MS6_1242
VCE: Vch1786_I0953(ctxA)
VCQ: EN18_10490
VCJ: VCD_000750
VCI: O3Y_06775
VCO: VC0395_0512(ctxA) VC0395_A1060(ctxA)
VCR: VC395_1571(ctxA) VC395_A0747(ctxA)
CDI: DIP0222(tox)
CDZ: CD31A_0221(tox)
CDS: CDC7B_0178(tox)
CDD: CDCE8392_0179(tox)
CDW: CDPW8_0179(tox1) CDPW8_0220(tox2)
COP: Cp31_0135(tox)
CUE: CULC0102_0213(tox)
CUN: Cul210932_0178(tox)
CUQ: Cul210931_0181(tox)
CUZ: Cul05146_0191(tox)
 » show all
Taxonomy
Reference
1  [PMID:6326138]
  Authors
Lee H, Iglewski WJ.
  Title
Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A.
  Journal
Proc Natl Acad Sci U S A 81:2703-7 (1984)
DOI:10.1073/pnas.81.9.2703
Reference
2  [PMID:3927821]
  Authors
Ueda K, Hayaishi O.
  Title
ADP-ribosylation.
  Journal
Annu Rev Biochem 54:73-100 (1985)
DOI:10.1146/annurev.bi.54.070185.000445
Other DBs
ExplorEnz - The Enzyme Database: 2.4.2.36
IUBMB Enzyme Nomenclature: 2.4.2.36
ExPASy - ENZYME nomenclature database: 2.4.2.36
BRENDA, the Enzyme Database: 2.4.2.36
CAS: 52933-21-8

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