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EC Tree
IUBMB Comments The reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10) .
The taxonomic range for the selected organisms is: Oryza sativa The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
udp-arabinopyranose mutase, cruam, osuam3, atrgp2, bdrgp1, atrgp1, osuam1,
more
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UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
in functional UDP-arabinopyranose mutases a specific arginyl residue is reversibly glycosylated. This arginyl residue together with a DXD motif is required for catalytic activity
UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
in functional UDP-arabinopyranose mutases a specific arginyl residue is reversibly glycosylated. This arginyl residue together with a DXD motif is required for catalytic activity
UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
the reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10)
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UDP-arabinopyranose pyranomutase
The reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10) [1].
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UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
UDP-beta-L-arabinopyranose
UDP-beta-L-arabinofuranose
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
in functional UDP-arabinopyranose mutases a specific arginyl residue is reversibly glycosylated. This arginyl residue together with a DXD motif is required for catalytic activity
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
the ratio of UDP-beta-L-arabinopyranose to UDP-beta-L-arabinofuranose reaches a plateau at 93:7 from both pyranose- and furanose-forming directions
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
in functional UDP-arabinopyranose mutases a specific arginyl residue is reversibly glycosylated. This arginyl residue together with a DXD motif is required for catalytic activity
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
the ratio of UDP-beta-L-arabinopyranose to UDP-beta-L-arabinofuranose reaches a plateau at 93:7 from both pyranose- and furanose-forming directions
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
the reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10)
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r
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
the reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10)
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UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
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r
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additional information
the enzyme does not require a cofactor
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additional information
the enzyme does not require a cofactor
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additional information
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the enzyme does not require a cofactor
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Mn2+
5 mM, activity almost doubles
additional information
no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
additional information
no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
additional information
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no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
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EDTA
5 mM, complete inhibition
UDP
competitive inhibition, lower affinity for enzyme than substrate
UDP-Gal
activity decreases by 40% under pretreatment for 3 h
UDP-Gal
decrease in mutase activity, when the nucleotide sugar reacts with the enzyme prior to the addition of beta-L-arabinofuranose
UDP-Glc
activity decreases by 40% under pretreatment for 3 h
UDP-Glc
decrease in mutase activity, when the nucleotide sugar reacts with the enzyme prior to the addition of beta-L-arabinofuranose
UDP-Xyl
activity decreases by 40% under pretreatment for 3 h
UDP-Xyl
decrease in mutase activity, when the nucleotide sugar reacts with the enzyme prior to the addition of beta-L-arabinofuranose
additional information
no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
-
additional information
no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
-
additional information
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no affect: CaCl2, MgCl2, CuSO4, ZnCl2, and CoCl2 at 5 mM
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additional information
the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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additional information
the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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additional information
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the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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additional information
the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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additional information
the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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additional information
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the combination of rUAM1, rUAM2, and rUAM3 increases activity 1.7fold as compared with that of the sum total of rUAM1, rUAM2, and rUAM3. This suggests that UAM isoenzymes work synergistically to increase activity
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0.0228
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
0.0454
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
0.0228 - 0.0531
UDP-beta-L-arabinofuranose
0.0454 - 0.055
UDP-beta-L-arabinopyranose
0.0228
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
0.0531
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
0.0454
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
0.055
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
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0.474
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
0.185
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
0.474
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
0.185
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
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20.8
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
40.8
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
20.8
UDP-beta-L-arabinofuranose
pH 6.8, 25°C
40.8
UDP-beta-L-arabinopyranose
pH 6.8, 25°C
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6
pyranose forming activity
6.5
furanose-forming activity
5.5 - 6
formation of beta-L-arabinofuranose
6
pyranose forming activity
6.5
furanose-forming activity
7 - 7.5
formation of beta-L-arabinopyranose
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4 - 8
pH 4.0: about 40% of maximal activity, pH 8.0: about 55% of maximal activity, pyranose forming activity
5 - 8
pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity, furanose-forming activity
4 - 8
pH 4.0: about 40% of maximal activity, pH 8.0: about 55% of maximal activity, pyranose forming activity
5 - 8
pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity, furanose-forming activity
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30 - 60
30°C: about 50% of maximal activity, 60°C: about 85% of maximal activity
30 - 60
30°C: about 50% of maximal activity, 60°C: about 85% of maximal activity
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UniProt
brenda
L. cv. Nihonbare
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
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RNAi is used to downregulate OsUAM gene expression. This leads to a reduction of between 6 and 44% in the amounts of arabinofuranose in the cell wall, a decrease in the extent of substitution of the xylan backbone, and a reduction of between 25% and 80% in the ferulic acid or p-coumaric acid contents of the wall. Transgenic rice plants with a >25% reduction in arabinose content are dwarfed and infertile
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40000
x * 40000, SDS-PAGE
41349
x * 41349, calculated from sequence
40000
x * 40000, SDS-PAGE
41000
x * 41000, SDS-PAGE
41349
x * 41349, calculated from sequence
460000
mutase is likely to exist as a complex composed of numerous proteins, gel filtration
additional information
native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
additional information
native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
additional information
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native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
additional information
native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
additional information
native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
additional information
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native mutase is likely to exist as a complex composed of several different UDP-arabinopyranose mutases
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?
x * 40000, SDS-PAGE
?
x * 41349, calculated from sequence
?
x * 40000, SDS-PAGE
?
x * 41349, calculated from sequence
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glycoprotein
autoglycosylation occurs at a specific arginyl residue in recombinant UDP-arabinopyranose mutase that is essential for mutase activity
glycoprotein
autoglycosylation occurs at a specific arginyl residue in recombinant UDP-arabinopyranose mutase that is essential for mutase activity
glycoprotein
rUAM1 is autoglycosylated when each protein reacts separately with UDP-Glc. Reversibly glycosylated in the presence of UDP-Glc
glycoprotein
rUAM3 is autoglycosylated when each protein reacts separately with UDP-Glc. Reversibly glycosylated in the presence of UDP-Glc
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R149A
activity is 154.1% of wild-type activity
R156A
activity is 0.1% of wild-type activity
R163A
activity is 2.0% of wild-type activity
D112N
activity is 131% of wild-type activity
R158A
activity is 5.7% of wild-type activity
R165A
activity is 131% of wild-type activity
R165K
activity is 131% of wild-type activity
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25
80 h, 50% loss of activity
50
1 h, 50% loss of activity
25
80 h, 50% loss of activity
50
1 h, 50% loss of activity
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rUMA1 expressed in insect cells retains activity after repeated cycles of freezing and thawing
repeated cycles of freezing and thawing did not significantly affect mutase activity
rUMA1 expressed in insect cells retains activity after repeated cycles of freezing and thawing
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-20°C, mutase activity is stable for at least 3 months
4°C, mutase activity is stable for 3 weeks
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expression in insect cells
expressed in Escherichia coli
expression in insect cells
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Konishi, T.; Miyazaki, Y.; Yamakawa, S.; Iwai, H.; Satoh, S.; Ishii, T.
Purification and biochemical characterization of recombinant rice UDP-arabinopyranose mutase generated in insect cells
Biosci. Biotechnol. Biochem.
74
191-194
2010
Oryza sativa (Q6Z4G3), Oryza sativa (Q8H8T0), Oryza sativa
brenda
Konishi, T.; Ohnishi-Kameyama, M.; Funane, K.; Miyazaki, Y.; Konishi, T.; Ishii, T.
An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation
Carbohydr. Res.
345
787-791
2010
Oryza sativa (Q6Z4G3), Oryza sativa (Q8H8T0), Oryza sativa
brenda
Konishi, T.; Takeda, T.; Miyazaki, Y.; Ohnishi-Kameyama, M.; Hayashi, T.; O'Neill, M.A.; Ishii, T.
A plant mutase that interconverts UDP-arabinofuranose and UDP-arabinopyranose
Glycobiology
17
345-354
2006
Oryza sativa (O82706), Oryza sativa (Q8H8T0), Oryza sativa
brenda
Konishi, T.; Aohara, T.; Igasaki, T.; Hayashi, N.; Miyazaki, Y.; Takahashi, A.; Hirochika, H.; Iwai, H.; Satoh, S.; Ishii, T.
Down-regulation of UDP-arabinopyranose mutase reduces the proportion of arabinofuranose present in rice cell walls
Phytochemistry
72
1962-1968
2011
Oryza sativa
brenda