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Literature summary for 1.3.99.B15 extracted from

  • Naparstek, S.; Guan, Z.; Eichler, J.
    A predicted geranylgeranyl reductase reduces the omega-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii (2012), Biochim. Biophys. Acta, 1821, 923-933.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor Haloferax volcanii although HVO_1799 contributes to dolichol phosphate omega-position isoprene reduction, the absence of HVO_1799 does not prevent N-glycosylation in Haloferax volcanii an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
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 ?
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor Haloferax volcanii DSM 3757 although HVO_1799 contributes to dolichol phosphate omega-position isoprene reduction, the absence of HVO_1799 does not prevent N-glycosylation in Haloferax volcanii an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
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 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GSC3 auxotrophic mutant WR536
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Haloferax volcanii DSM 3757 D4GSC3 auxotrophic mutant WR536
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor although HVO_1799 contributes to dolichol phosphate omega-position isoprene reduction, the absence of HVO_1799 does not prevent N-glycosylation in Haloferax volcanii Haloferax volcanii an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
-
 ?
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor the enzyme contributes to dolichol phosphate omega-position isoprene reduction. The actual substrate used by this enzyme has not been experimetally determined Haloferax volcanii an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
-
 ?
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor although HVO_1799 contributes to dolichol phosphate omega-position isoprene reduction, the absence of HVO_1799 does not prevent N-glycosylation in Haloferax volcanii Haloferax volcanii DSM 3757 an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
-
 ?
an archaeal alpha-reduced dolichyl phosphate + reduced acceptor the enzyme contributes to dolichol phosphate omega-position isoprene reduction. The actual substrate used by this enzyme has not been experimetally determined Haloferax volcanii DSM 3757 an archaeal alpha,omega-reduced dolichyl phosphate + acceptor
-
 ?

Synonyms

Synonyms Comment Organism
DolP omega-isoprene reductase
-
 Haloferax volcanii
HVO_1799 locus name Haloferax volcanii

General Information

General Information Comment Organism
malfunction cells deleted of HVO_1799 fail to fully reduce the isoprene chains of membrane phospholipids and glycolipids. The absence of HVO_1799 leads to a loss of saturation of the omega-position isoprene subunit of C55 and C60 dolichol phosphate, with the effect of HVO_1799 deletion being more pronounced with C60 dolichol phosphate than with C55 dolichol phosphate. Glycosylation of dolichol phosphate in the deletion strain occurred preferentially on that version of the lipid saturated at both the alpha- and omega-position isoprene subunits Haloferax volcanii