Enzymes
UniProtKB help_outline | 4 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
diphthamide-[translation elongation factor 2]
Identifier
RHEA-COMP:10174
Reactive part
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- Name help_outline diphthamide residue Identifier CHEBI:16692 Charge 1 Formula C13H22N5O2 SMILEShelp_outline C[N+](C)(C)[C@@H](CCc1nc(C[C@H](N-*)C(-*)=O)c[nH]1)C(N)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,186 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Identifier
RHEA-COMP:10175
Reactive part
help_outline
- Name help_outline N-(ADP-D-ribosyl)diphthamide residue Identifier CHEBI:82697 Charge -1 Formula C28H41N10O15P2 SMILEShelp_outline C[N+](C)(C)[C@@H](CCc1nc(C[C@H](N-*)C(-*)=O)cn1[C@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O)C(N)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nicotinamide Identifier CHEBI:17154 (Beilstein: 383619; CAS: 98-92-0) help_outline Charge 0 Formula C6H6N2O InChIKeyhelp_outline DFPAKSUCGFBDDF-UHFFFAOYSA-N SMILEShelp_outline NC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 61 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:11820 | RHEA:11821 | RHEA:11822 | RHEA:11823 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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ADP-ribosylation.
Ueda K., Hayaishi O.
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Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A.
Lee H., Iglewski W.J.
An ADP-ribosyltransferase was found in elongation factor 2 (EF-2) preparations from polyoma virus-transformed baby hamster kidney (pyBHK) cells. Like fragment A of diphtheria toxin and Pseudomonas toxin A, this eukaryotic cellular enzyme transfers [14C]adenosine from NAD+ to EF-2. However, the cel ... >> More
An ADP-ribosyltransferase was found in elongation factor 2 (EF-2) preparations from polyoma virus-transformed baby hamster kidney (pyBHK) cells. Like fragment A of diphtheria toxin and Pseudomonas toxin A, this eukaryotic cellular enzyme transfers [14C]adenosine from NAD+ to EF-2. However, the cellular transferase is immunologically distinct from fragment A. The transferase also can be distinguished from fragment A and Pseudomonas toxin A by the inhibition of the activity of the former by cytoplasmic extracts and by histamine. Snake venom phosphodiesterase digestion of the [14C]adenosine-labeled EF-2 product of the cellular transferase reaction yielded [14C]AMP, indicating that the cellular enzyme is a mono(ADP-ribosyl)transferase. The forward ADP-ribosylation reaction catalyzed by the cellular enzyme is reversed by fragment A, yielding [14C]NAD+. The results strongly suggest that the cellular transferase is a mono(ADP-ribosyl)transferase, which ADP-ribosylates the same diphthamide residue of EF-2 as does fragment A and Pseudomonas toxin A. << Less
Proc Natl Acad Sci U S A 81:2703-2707(1984) [PubMed] [EuropePMC]
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Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae.
Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H., Merrill A.R.
The ADP-ribosyltransferases are a class of enzymes that display activity in a variety of bacterial pathogens responsible for causing diseases in plants and animals, including those affecting mankind, such as diphtheria, cholera, and whooping cough. We report the characterization of a novel toxin f ... >> More
The ADP-ribosyltransferases are a class of enzymes that display activity in a variety of bacterial pathogens responsible for causing diseases in plants and animals, including those affecting mankind, such as diphtheria, cholera, and whooping cough. We report the characterization of a novel toxin from Vibrio cholerae, which we call cholix toxin. The toxin is active against mammalian cells (IC(50) = 4.6 +/-0.4 ng/ml) and crustaceans (Artemia nauplii LD(50) = 10 +/-2 mug/ml). Here we show that this toxin is the third member of the diphthamide-specific class of ADP-ribose transferases and that it possesses specific ADP-ribose transferase activity against ribosomal eukaryotic elongation factor 2. We also describe the high resolution crystal structures of the multidomain toxin and its catalytic domain at 2.1- and 1.25-A resolution, respectively. The new structural data show that cholix toxin possesses the necessary molecular features required for infection of eukaryotes by receptor-mediated endocytosis, translocation to the host cytoplasm, and inhibition of protein synthesis by specific modification of elongation factor 2. The crystal structures also provide important insight into the structural basis for activation of toxin ADP-ribosyltransferase activity. These results indicate that cholix toxin may be an important virulence factor of Vibrio cholerae that likely plays a significant role in the survival of the organism in an aquatic environment. << Less