- NAD(+)—diphthamide ADP-ribosyltransferase
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NAD+-diphthamide ADP-ribosyltransferase Identifiers EC number 2.4.2.36 CAS number 52933-21-8 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / EGO Search PMC articles PubMed articles In enzymology, a NAD+-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) is an enzyme that catalyzes the chemical reaction
- NAD+ + peptide diphthamide nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide
Thus, the two substrates of this enzyme are NAD+ and peptide diphthamide, whereas its two products are nicotinamide and peptide N-(ADP-D-ribosyl)diphthamide.
This enzyme belongs to the family of glycosyltransferases, to be specific, the pentosyltransferases. The systematic name of this enzyme class is NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase. Other names in common use include ADP-ribosyltransferase, mono(ADPribosyl)transferase, and NAD-diphthamide ADP-ribosyltransferase.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1S5B, 1S5C, 1S5D, 1S5E, 1S5F, 1SGK, 1TOX, 1XDT, 1XK9, 1ZM3, 1ZM4, 1ZM9, 2A5D, 2A5F, and 2A5G.
References
- Lee H, Iglewski WJ (1984). "Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A". Proc. Natl. Acad. Sci. U. S. A. 81 (9): 2703–7. doi:10.1073/pnas.81.9.2703. PMC 345138. PMID 6326138. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=345138.
- Ueda K, Hayaishi O (1985). "ADP-ribosylation". Annu. Rev. Biochem. 54 (1): 73–100. doi:10.1146/annurev.bi.54.070185.000445. PMID 3927821.
See also
2.4.2: Pentosyl-
transferasesOtherOther2.4.99: Sialyl
transferasesB enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6 Categories:- Enzyme stubs
- EC 2.4.2
- NADH-dependent enzymes
- Enzymes of known structure
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