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
2016
cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases*
Grabińska K, Park EJ, Sessa WC. cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases*. Journal Of Biological Chemistry 2016, 291: 18582-18590. PMID: 27402831, PMCID: PMC5000101, DOI: 10.1074/jbc.r116.739490.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsDimethylallyltranstransferaseHemiterpenesHumansOrganophosphorus CompoundsPlant ProteinsProtein BiosynthesisRubberConceptsUndecaprenyl diphosphate synthaseIsopentenyl diphosphateDomains of lifeConsecutive condensation reactionsPlant orthologsHeteromeric enzymeCis-PrenyltransferasesDiphosphate synthaseProtein glycosylationPolyprenyl diphosphateBacterial enzymesHuman diseasesMode of actionLarge familyOrthologsEnzymeRubber synthesisSubunitsNew insightsCarbon skeletonStructural componentsDiphosphateMammalsFungalGlycosylation