Information on EC 4.2.1.76 - UDP-glucose 4,6-dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.76
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RECOMMENDED NAME
GeneOntology No.
UDP-glucose 4,6-dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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NIL
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UDP-beta-L-rhamnose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4,6-hydro-lyase (UDP-4-dehydro-6-deoxy-D-glucose-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
68189-53-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCV-1, two UGD isozymes, gene Z544R, propagated in Chlorella strain SAG 3.83
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
red campion
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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inactivation of GAL102-encoded UDP-glucose 4,6-dehydratase activity causes altered mannosylation of cell wall proteins, loss of cell wall integrity and changes in biofilm characteristics. The reduced virulence of gal102-deficient Candida albicans is associated with ist inability to elicit a strong pro-inflammatory response
physiological function
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UDP-glucose 4, 6-dehydratase activity plays an important role in maintaining cell wall integrity and virulence of Candida albicans
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-D-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
UDP-D-glucose
?
show the reaction diagram
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biosynthesis of UDP-L-rhamnose from UDP-D-glucose
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UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose
show the reaction diagram
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?
UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
UDP-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
additional information
?
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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
dTDP-D-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
UDP-D-glucose
?
show the reaction diagram
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biosynthesis of UDP-L-rhamnose from UDP-D-glucose
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UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
UDP-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-chloromercuribenzoate
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UDP
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1 mM, 41% inhibition of purified His6-tagged RHM2-N protein is inhibited
UDP-L-rhamnose
UDP-Rha
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1 mM, 82% inhibition of purified His6-tagged RHM2-N protein
UDP-Xyl
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1 mM, 79% inhibition of purified His6-tagged RHM2-N protein is inhibited
UMP
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1 mM, 23% inhibition of purified His6-tagged RHM2-N protein is inhibited
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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mimivirus UGD requires exogenous NAD+ for activity during purification
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0184 - 0.116
UDP-D-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2860
UDP-D-glucose
Arabidopsis thaliana
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recombinant RHM2-N protein (amino acids 1–370)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0042
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purified UGD, pH 7.5-8.5, 25°C, 0.1 mM NAD+
0.023
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purified ATCV-1 UGD, pH 7.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9.8
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half maximum velocities at
6.5 - 8
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pH 6.5: about 40% of maximal activity, pH 8.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
38
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enzyme assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
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25°C: about 50% of maximal activity, 45°C: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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x * 33000, UGER, SDS-PAGE
37000
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2 * 37000, UGD, SDS-PAGE
39000
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2 * 39000, UGD, SDS-PAGE
47000
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UGER, gel filtration
52000
3 * 52000, SDS-PAGE
52500
3 * 52500, SDS-PAGE
75000
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UGD, gel filtration
100000
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UGD, gel filtration
140000
additional information
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RHM2/MUM4 is a trifunctional enzyme with UDP-D-glucose 4,6-dehydratase, UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase, and UDP-4-keto-L-rhamnose 4-keto-reductase activities. The N-terminal region of RHM2 (RHM2-N: amino acids 1-370) has the first activity and the C-terminal region of RHM2 (RHM2-C: amino acids 371-667) has the two following activities
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
monomer or dimer
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x * 33000, UGER, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-Sepharose column chromatography
partial
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recombinant GST-tagged isozymes from Escherichia coli by glutathione affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expression in Saccharomyces cerevisae; expression in Saccharomyces cerevisae. Recombinant His6-tagged RHM2-N protein (amino acids 1-370). The RHM2/MUM4 protein is more stable than RHM1 or RHM3 in yeast cells
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gene R141, transcription profiling of UGD, phylogenetic analysis
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gene Z544R, UGD transcription profiling, phylogenetic analysis, expression of the two GST-tagged UGD isozymes in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D96N
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mutation completely abolishes UDP-Glc 4,6-dehydratase activity
G18A
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mutation completely abolishes UDP-Glc 4,6-dehydratase activity
G193R
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mutation completely abolishes UDP-Glc 4,6-dehydratase activity
K165A
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mutation completely abolishes UDP-Glc 4,6-dehydratase activity
K35A
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activity of the mutant is lower than activity of wild-type enzyme