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IUBMB Comments Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, but more slowly.
2.4.1.78
neuregulins
schizophrenia
interneurons
nrg1-erbb4
juxtamembrane
heregulin
nrg1-induced
parvalbumin-positive
pdgfr-beta
betacellulin
Synonyms
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glucosyltransferase, uridine diphosphoglucose-polyprenol monophosphate
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UDP-glucose:polyprenol monophosphate glucosyltransferase
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UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose
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hexosyl group transfer
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UDP-glucose:phosphopolyprenol D-glucosyltransferase
Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, but more slowly.
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UDP-glucose + ficaprenol phosphate
UDP + ficaprenolphosphate-glucose
UDP-glucose + ficaprenol phosphate
UDP + ficaprenolphosphate-glucose
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Substrates: i.e. mixture of C50, C55 and C66 cis- and trans-polyprenols, most effective lipid glucosylacceptor, phosphate esters of phytol, betulaprenol, mixture of C30-C45 cis- and trans-polyprenols and solanesol, C45 all-trans polyprenol and dolichol, mainly C95 cis- and trans-polyprenols, containing saturated alpha-isoprene residue are poor substrates, UDP-galactose replaces UDP-glucose with crude membrane-preparations, but the product is ficaprenolphosphate-glucose. No substrates are GDP-mannose, UDP-glucuronic acid and UDP-N-acetylglucosamine
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UDP-glucose + ficaprenol phosphate
UDP + ficaprenolphosphate-glucose
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Substrates: -
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UDP-glucose + ficaprenol phosphate
UDP + ficaprenolphosphate-glucose
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Substrates: -
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deoxycholate
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stimulates solubilized activity
taurocholate
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stimulates solubilized activity
Triton X-100
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stimulates solubilized activity
additional information
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androgenic stimulation
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strain 2a, not strain Y
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brenda
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Highest Expressing Human Cell Lines
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Triton X-100, taurocholate or deoxycholate stabilizes
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Jankowski, W.; Mankowski, T.; Chojnacki, T.
Formation of polyprenol monophosphate glucose in Shigella flexneri
Biochim. Biophys. Acta
337
153-162
1974
Shigella flexneri
brenda
Iusem, N.D.; De Larminat, M.A.; Tezon, J.G.; Blaquier, J.A.; Belocopitow, E.
Androgen dependence of protein N-glycosylation in rat epididymis
Endocrinology
114
1448-1453
1984
Rattus norvegicus
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