Information on EC 2.4.1.264 - D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase

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The expected taxonomic range for this enzyme is: Xanthomonas

EC NUMBER
COMMENTARY hide
2.4.1.264
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RECOMMENDED NAME
GeneOntology No.
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol = UDP + D-GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetan biosynthesis
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xanthan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate:D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 2-beta-glucuronyltransferase
The enzyme is involved in the biosynthesis of the exopolysaccharides xanthan (in the bacterium Xanthomonas campestris) and acetan (in the bacterium Gluconacetobacter xylinus).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pv. oryzae
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
show the reaction diagram
UDP-glucuronate + 6-O-acetyl-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
UDP + GlcA-beta-(1->2)-(6-O-acetyl)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
show the reaction diagram
GumK shows diminished activity with 6-O-acetyl-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol, a putative intermediate in the synthesis of xanthan. This indicates that acetylation of the internal mannose takes place after the formation of the GumK product
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UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
show the reaction diagram
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
UDP + GlcA-beta-(1-2)-D-Man-alpha-(1-3)-D-Glc-beta-(1-4)-D-Glc-alpha-1-diphosphoundecaprenol
show the reaction diagram
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
show the reaction diagram
additional information
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GumK undergoes a conformational change upon donor substrate binding, likely bringing the two Rossmann fold domains closer together and triggering a change in the N-terminal domain, with consequent generation of the acceptor substrate binding site
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
show the reaction diagram
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GumK 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, UDP-glucuronic acid, and GDP-mannose onto a polyprenol phosphate carrier, by the glycosyltransferase homologues encoded by the gumD, gumM, gumH, gumK, and gumI genes, respectively
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UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
show the reaction diagram
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the enzyme is involved in biosynthesis of xanthan
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UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.194 - 0.39
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
0.06 - 1.19
UDP-glucuronate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 0.088
UDP-glucuronate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 1.42
UDP-glucuronate
226
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 44000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, crystal structure of apo-enzyme at 1.9 A resolution, and of enzyme in complex with UDP, at 2.28 A resolution. Residue Asp157 serves as the general base in the transfer reaction. Residues M231, M273, E272, Y292, M306, K307, and Q310 interact with UDP. Cocrystallisation of GumK or mutant D157A in presence of UDP-glucuronate is not possible
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hanging-drop vapour diffusion method, crystals of recombinant GumK, 1.9 A resolution
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in silico-built models of GumK complexed with UDP-GlcA as well as its analogs UDP-glucose and UDP-galacturonic acid. UDP-GlcA binding to GumK triggers a change in the GumK tertiary structure, affecting N-terminal hydrophobic residues to generate or improve the lipid-derived acceptor substrate site, while UDP-GlcA accommodates the transfer reaction
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D157A
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mutation in UDP binding site, loss of activity
D157E
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mutation in UDP binding site, loss of activity
D157N
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mutation in UDP binding site, loss of activity
D207A
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mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value
D234A
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mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value
E192A
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mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value
E272A
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mutation in UDP binding site, kcat/KM is 4.6fold lower than wild-type value
E272D
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mutation in UDP binding site, kcat/KM is 2fold lower than wild-type value
K307A
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mutation in UDP binding site, kcat/KM is 560fold lower than wild-type value
M231A
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mutation in UDP binding site, kcat/Km for UDP-glucuronate is similar to wild-type value
Q310A
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mutation in UDP binding site, kcat/KM is 22.2fold lower than wild-type value
Y292A
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mutation in UDP binding site, kcat/KM is 14.7fold lower than wild-type value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis