Diphthamide Contents Structure Biological function Biosynthesis References Navigation...
Amino acidsImidazolesQuaternary ammonium compoundsPosttranslational modificationZwitterions
histidineamino acideukaryotic elongation factor 2X-ray crystallographyNF-κBS-adenosyl methionine
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IUPAC name 2-Amino-3-[2-(3-carbamoyl-3-trimethylammonio-propyl)-3H-imidazol-4-yl]propanoate | |
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Chemical formula | C13H23N5O3 |
Molar mass | 297.354 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
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Diphthamide is a post-translationally modified histidine amino acid found in archaeal and eukaryotic elongation factor 2 (eEF-2).
Contents
1 Structure
2 Biological function
3 Biosynthesis
4 References
Structure
Diphthamide is proposed to be a 2-[3-carboxyamido-3-(trimethylammonio)propyl histidine. Though this structure has been confirmed by X-ray crystallography, its stereochemistry is uncertain.[1]
Biological function
Diphthamide ensures translation fidelity.[2]
The presence or absence of diphthamide is known to affect NF-κB or death receptor pathways.[3]
Biosynthesis
Diphthamide is biosynthesized from histidine and S-adenosyl methionine.[2]
References
^ Jorgensen, R (2006). "The life and death of translation elongation factor 2". Biochem Soc Trans. 34: 1–6. doi:10.1042/BST20060001. PMID 16246167..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .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 .citation .cs1-lock-limited a,.mw-parser-output .citation .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 .citation .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-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.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}
^ ab Su, Xiaoyang; Lin, Zhewang; Lin, Hening (2013-11-01). "The biosynthesis and biological function of diphthamide". Critical Reviews in Biochemistry and Molecular Biology. 48 (6): 515–521. doi:10.3109/10409238.2013.831023. ISSN 1040-9238. PMC 4280834. PMID 23971743.
^ Stahl, Sebastian (2015). "Loss of diphthamide pre-activates NF-κB and death receptor pathways and renders MCF7 cells hypersensitive to tumor necrosis factor". Proc Natl Acad Sci U S A. 112: 10732–7. doi:10.1073/pnas.1512863112. PMC 4553792. PMID 26261303.
