Characterization of the Saccharomyces cerevisiae cis-prenyltransferase required for dolichyl phosphate biosynthesis
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Investigation of the conserved reentrant membrane helix in the monotopic phosphoglycosyl transferase superfamily supports key molecular interactions with polyprenol phosphate substrates
2019, Archives of Biochemistry and BiophysicsCitation Excerpt :The precise structural features of the PrenPs used in glycan assembly vary by species (Fig. 1A). Archaea and eukaryotes utilize α-saturated polyprenol phosphates, called dolichols, which range in length from as few as eight isoprene units in some archaea, to 20 or more in mammals and plants [5–9]. Archaeal PrenPs can be additionally saturated at other isoprene units [10,11].
A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity
2017, Journal of Biological ChemistryCitation Excerpt :As judged by SDS-PAGE and Coomassie staining of each fraction, the hCIT–NgBR complex was ∼95% pure (Fig. 2C), and the purified heteromeric complex ran as monodispersed peak on size-exclusion chromatography (Fig. 2D, solid line) that tracked with cis-PT activity (Fig. 2D, dashed line). The purified hCIT–NgBR complex required Mg2+ for its activity consistent with previous studies in bacterial and eukaryotic enzymes (23–29) with maximum activity attained at 0.5–2.0 mm MgCl2. ( Fig. 3A).
Purification and characterization of human dehydrodolychil diphosphate synthase (DHDDS) overexpressed in E. coli
2017, Protein Expression and PurificationCIS-Prenyltransferase: New insights into protein glycosylation, rubber synthesis, and human diseases
2016, Journal of Biological ChemistryCitation Excerpt :While searching for the enzymatic machinery involved in the formation of crucial intermediates in bacterial cell wall synthesis, researchers discovered UPPS over 40 years ago (6–12). Following the studies in bacteria, a description of an ER-localized enzymatic activity was discovered in mammals and in yeast (13–15). UPPS utilizes FPP as a substrate to sequentially add eight IPP units to form undecaprenyl diphosphate (C11).
Protein O-mannosylation: What we have learned from baker's yeast
2013, Biochimica et Biophysica Acta - Molecular Cell ResearchAt the membrane frontier: A prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl-phosphates
2012, Archives of Biochemistry and BiophysicsCitation Excerpt :This general pathway is responsible for the production of a wide range of polyprenol structures, which vary in length across organisms, ranging from an average of C55 polyprenols in bacteria and C95 dolichols in mammals to C200 polyprenols in plants (Table 1). Bacteria typically exploit undecaprenol, a C55 unsaturated polyprenol [14], while archaeal organisms typically contain C55–C65 dolichols [15], Saccharomyces cerevisiae (yeast) contain C70–C80 dolichols [16] and mammalian tissues contain C90–C100 dolichols (Table 1) [17]. In addition, unusual polyprenols that include additional saturated isoprene units at the ω-terminus have been identified in Mycobacterium [18,19] as well as the archaeal species, Haloferex volcanii [20] and Sulfolobus acidocaldarious [21].