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NAD(+)—diphthamide ADP-ribosyltransferase








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 / QuickGO

















In enzymology, a NAD+-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) is an enzyme that catalyzes the chemical reaction


NAD+ + peptide diphthamide ⇌{displaystyle rightleftharpoons }rightleftharpoons 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[edit]


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[edit]






  • 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&ndash, 7. doi:10.1073/pnas.81.9.2703. PMC 345138. PMID 6326138..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  • Ueda K, Hayaishi O (1985). "ADP-ribosylation". Annu. Rev. Biochem. 54 (1): 73&ndash, 100. doi:10.1146/annurev.bi.54.070185.000445. PMID 3927821.



See also[edit]


  • Diphtheria toxin











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