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IUBMB Commentscis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates.
The enzyme appears in viruses and cellular organisms
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UDP-glucose + cis-p-coumarate = 4'-O-beta-D-glucosyl-cis-p-coumarate + UDP
cis-caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates
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hexosyl group transfer
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UDP-glucose:cis-p-coumarate beta-D-glucosyltransferase
cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates.
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cis-caffeic acid + UDP-glucose + H2O
4'-O-beta-D-glucosyl-cis-caffeate + UDP
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enzyme activity of 10% compared with that using cis-p-coumaric acid as substrate
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cis-p-coumarate + UDP-glucose + H2O
4'-O-beta-D-glucosyl-cis-p-coumarate + UDP
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UDP-glucose + cis-coniferyl alcohol + H2O
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UDP-glucose + cis-p-coumarate
4'-O-beta-D-glucosyl-cis-p-coumarate + UDP
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UDP-glucose + cis-p-coumarate + H2O
4'-O-beta-D-glucosyl-cis-p-coumarate + UDP
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UDP-glucose + cis-coniferyl alcohol + H2O
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UDP-glucose + cis-p-coumarate + H2O
4'-O-beta-D-glucosyl-cis-p-coumarate + UDP
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2-mercaptoethanol
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14 mM, 30% inhibition
cis-p-coumaric acid
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inhibits the rection above 1 mM concentration
NaCl
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0.4 M, 40% inhibition
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0.044
cis-p-coumarate
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0.11
UDP-glucose
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cosubstrate
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american beech
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brenda
peat moss
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brenda
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7.8 - 9.5
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below pH 7.8 and above pH 9.5 rapid drop in enzyme activity
288689
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-18°C, freezing results in a loss of activity of more than 50%
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4°C, loses more than 25% of its activity within 24 h, 5% glycerol causes total loss of activity after 48 h
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Rasmussen, S.; Rudolph, H.
Isolation, purification and characterization of UDP-glucose:cis-p-coumaric acid-beta-D-glucosyltransferase from Sphagnum fallax
Phytochemistry
46
449-453
1997
Fagus grandifolia, Sphagnum fallax
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brenda
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