2017
A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity
Grabińska KA, Edani BH, Park EJ, Kraehling JR, Sessa WC. A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity. Journal Of Biological Chemistry 2017, 292: 17351-17361. PMID: 28842490, PMCID: PMC5655512, DOI: 10.1074/jbc.m117.806034.Peer-Reviewed Original ResearchConceptsUndecaprenyl diphosphate synthaseDiphosphate synthaseDomains of lifeProtein glycosylation reactionsStrong conservationCellular functionsG motifTerminal tailPrenyltransferase activityFirst enzymeCis-prenyltransferaseBacterial enzymesIsoprene unitsSubunitsLarge familyNgBREnzyme activityG sequencesEnzymeDolichyl phosphateMotifSynthaseEukaryotesOrthologsArchaea
2010
Molecular characterization of the cis-prenyltransferase of Giardia lamblia
Grabińska K, Cui J, Chatterjee A, Guan Z, Raetz C, Robbins P, Samuelson J. Molecular characterization of the cis-prenyltransferase of Giardia lamblia. Glycobiology 2010, 20: 824-832. PMID: 20308470, PMCID: PMC2900897, DOI: 10.1093/glycob/cwq036.Peer-Reviewed Original ResearchConceptsIsoprene unitsDouble deletion mutantGPI anchor synthesisMost eukaryotesHigher eukaryotesAnchor synthesisN-glycosylationGlycosylphosphatidylinositol (GPI) anchorCis-prenyltransferaseKinase activityPolyprenyl pyrophosphateBacterial enzymesDolichol kinase activityDolichol kinaseMolecular characterizationImportant enzymeN-glycansEukaryotesProtistsPolyprenol lipidsNormal growthPyrophosphate linkageEnzymeGiardia lambliaDolichol