Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae
Kim, S.Y.; Kim, J.G.; Lee, B.M.; Cho, J.Y.; Biotechnol. Lett. 31, 265-270 (2008) 
Data extracted from this reference:
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
UDP-glucose + ditrans,octacis-undecaprenyl phosphate
Xanthomonas oryzae
GumD is involved in biosynthesis of the pentasaccharide repeating unit of xanthan. It is suggested that the wild-type Xanthomonas oryzae-produced xanthan is assembled by the sequential addition of UDP-glucose, UDP-glucose, GDP-mannose, UDPglucuronic acid, and GDP-mannose onto a polyprenol phosphate carrier, by the glycosyltransferase homologues encoded by the gumD, gumM, gumH, gumK, and gumI genes, respectively
UMP + alpha-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Xanthomonas oryzae
-
pv. oryzae
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
UDP-glucose + ditrans,octacis-undecaprenyl phosphate
GumD is involved in biosynthesis of the pentasaccharide repeating unit of xanthan. It is suggested that the wild-type Xanthomonas oryzae-produced xanthan is assembled by the sequential addition of UDP-glucose, UDP-glucose, GDP-mannose, UDPglucuronic acid, and GDP-mannose onto a polyprenol phosphate carrier, by the glycosyltransferase homologues encoded by the gumD, gumM, gumH, gumK, and gumI genes, respectively
702828
Xanthomonas oryzae
UMP + alpha-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
gumD
-
Xanthomonas oryzae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
UDP-glucose + ditrans,octacis-undecaprenyl phosphate
Xanthomonas oryzae
GumD is involved in biosynthesis of the pentasaccharide repeating unit of xanthan. It is suggested that the wild-type Xanthomonas oryzae-produced xanthan is assembled by the sequential addition of UDP-glucose, UDP-glucose, GDP-mannose, UDPglucuronic acid, and GDP-mannose onto a polyprenol phosphate carrier, by the glycosyltransferase homologues encoded by the gumD, gumM, gumH, gumK, and gumI genes, respectively
UMP + alpha-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
UDP-glucose + ditrans,octacis-undecaprenyl phosphate
GumD is involved in biosynthesis of the pentasaccharide repeating unit of xanthan. It is suggested that the wild-type Xanthomonas oryzae-produced xanthan is assembled by the sequential addition of UDP-glucose, UDP-glucose, GDP-mannose, UDPglucuronic acid, and GDP-mannose onto a polyprenol phosphate carrier, by the glycosyltransferase homologues encoded by the gumD, gumM, gumH, gumK, and gumI genes, respectively
702828
Xanthomonas oryzae
UMP + alpha-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
significantly attenuated production of xanthan in knock-out mutant strain SJ1017
Xanthomonas oryzae
physiological function
GumH is involved in biosynthesis of the pentasaccharide repeating unit of xanthan
Xanthomonas oryzae
General Information (protein specific)
General Information
Commentary
Organism
malfunction
significantly attenuated production of xanthan in knock-out mutant strain SJ1017
Xanthomonas oryzae
physiological function
GumH is involved in biosynthesis of the pentasaccharide repeating unit of xanthan
Xanthomonas oryzae
Other publictions for EC 2.7.8.31
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
722853
Schatschneider
Establishment, in silico analy ...
Xanthomonas campestris pv. campestris, Xanthomonas campestris pv. campestris B100
J. Biotechnol.
167
123-134
2013
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723608
Zhang
The HD-GYP domain protein RpfG ...
Xanthomonas oryzae pv. oryzicola
PLoS ONE
8
e59428
2013
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722541
Patel
Functional characterization of ...
Caulobacter vibrioides, Escherichia coli, Caulobacter vibrioides CB15
J. Bacteriol.
194
2646-2657
2012
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702828
Kim
Mutational analysis of the gum ...
Xanthomonas oryzae
Biotechnol. Lett.
31
265-270
2008
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2
2
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701945
Dunger
Xanthan is not essential for p ...
Xanthomonas axonopodis
Arch. Microbiol.
188
127-135
2007
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713218
Kemp
Xanthomonas axonopodis pv. man ...
Xanthomonas phaseoli pv. manihotis
Physiol. Mol. Plant Pathol.
64
209-218
2004
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3
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704257
Katzen
Xanthomonas campestris pv. cam ...
Xanthomonas campestris
J. Bacteriol.
180
1607-1617
1998
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702006
Chou
The Xanthomonas campestris gum ...
Xanthomonas campestris
Biochem. Biophys. Res. Commun.
233
265-269
1997
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704251
Pollock
Mechanism of bacitracin resist ...
Xanthomonas campestris
J. Bacteriol.
176
6229-6237
1994
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704249
Ielpi
Sequential assembly and polyme ...
Xanthomonas campestris
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