- Dolichylation
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In biochemistry, dolichylation is the covalent addition of a dolichol group to a protein.[1] This post-translational modification has been shown to occur in a number of eukaryotes, including the malarial parasite Plasmodium falciparum.[2]
References
- ^ Hjertman, M.; Wejde, J.; Dricu, A.; Carlberg, M.; Griffiths, W. J.; Sjövall, J.; Larsson, O. (1997). "Evidence for protein dolichylation". FEBS letters 416 (3): 235–238. PMID 9373159.
- ^ Dalexandri, F.; Kimura, E.; Peres, V.; Katzin, A. (2006). "Protein dolichylation in Plasmodium falciparum". FEBS Letters 580 (27): 6343–6348. doi:10.1016/j.febslet.2006.10.042. PMID 17084391.
Protein primary structure and posttranslational modifications General N terminus C terminus Single specific AAs Phosphorylation · Sulfation · Porphyrin ring linkage · Adenylylation · Flavin linkage · Topaquinone (TPQ) formationAspartateGlutamateTransglutaminationMethylation · Acetylation · Acylation · Adenylylation · Hydroxylation · Ubiquitination · Sumoylation · ADP-ribosylation · Deamination · Oxidative deamination to aldehyde · O-glycosylation · Imine formation · Glycation · CarbamylationDiphthamide formation · AdenylylationCrosslinks between two AAs Sulfilimine bondLysine-TyrosylquinoneLysine tyrosylquinone (LTQ) formationTryptophan-TryptophylquinoneThree consecutive AAs
(Chromophore formation)4-(p-hydroxybenzylidene)-5-imidazolinone formationCrosslinks between four AAs Secondary structure→Categories:
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