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Enzyme Nomenclature
Information on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.22
Word Map on EC 1.1.1.22
- 1.1.1.22
-
udp-glucuronic
- polysaccharide
- glycosaminoglycans
- hyaluronan
- udp-xylose
-
pyrophosphorylase
-
glucuronidation
-
exopolysaccharide
-
glucuronic
- udp-glca
- udp-sugars
-
udp-glucuronyltransferase
- udp-d-glucuronate
-
udpga
- medicine
- synthesis
- pharmacology
- molecular biology
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.22
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RECOMMENDED NAME
GeneOntology No.
UDP-glucose 6-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
ping-pong reaction mechanism
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
also shows alcohol dehydrogenase activity
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UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
also shows alcohol dehydrogenase activity; also shows aldehyde dehydrogenase activity; reaction mechanism, C275 provides SH-group in the catalytic centre
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UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
two-step reaction, reaction mechanism
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UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
bi-uni-uni-bi mechanism
Saccharum spp.
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
mechanism, ordered water molecule H-bonded to T118 serves as catalytic base in hydride transfer
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UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is also binds RNA and acts as a ribonuclease
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is also binds RNA and acts as a ribonuclease
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UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:NAD+ 6-oxidoreductase
Also acts on UDP-alpha-D-2-deoxyglucose.
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CAS REGISTRY NUMBER
COMMENTARY
9028-26-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
originally isolated from the lymph nodes of patients with chronic granulomatous disease (CGD)
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-
two-dimensional IEF SDS-PAGE showed several isoforms of the purified enzyme
-
-
induction by short-term feeding with sucrose, sorbitol, ethylene glycol or light exposure
SwissProt
syncytia induced by nematode Heterodera schachtii
UniProt
overexpression of enzyme plus transformation of gene cluster for K5 polysaccharide production
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isoform PA3559, expressed primarily in low concentrations of Mg2+
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the the UGDH family of proteins
evolution
the N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily
evolution
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the N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily
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malfunction
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Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
malfunction
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UGDH specific siRNAs markedly inhibits UGDH mRNA and protein expression, and leads to an obvious suppression of proteoglycans synthesis in human articular chondrocytes. UGDH protein level in human osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis. Interleukin-1beta inhibits UGDH gene expression through modulating UGDH transregulators and the downstream signaling cascades, including the SAP/JNK and p38 MAPK pathways which might be involved in the proteoglycans loss of osteoarthritis cartilage and contribute to the osteoarthritis pathogenesis
malfunction
UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
malfunction
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mutant dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. The purified enzymes reveal a significant decrease in the enzymatic activity of the obligate dimer and hexamer mutants. Both T325A and T325D mutants were significantly less efficient in promoting downstream hyaluronan production by HEK293 cells
malfunction
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Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
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malfunction
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UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
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metabolism
the enzyme participates in sucrose/polysaccharide metabolism and cell wall biosynthesis
metabolism
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in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
metabolism
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in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
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physiological function
UDP-glucose dehydrogenase is responsible for the NAD-dependent twofold oxidation of UDP-glucose to UDP-glucuronic acid, one of the key components for gellan biosynthesis
physiological function
-
UGDH oxidizes UDP-glucose to UDP-glucuronate, an essential precursor for production of hyaluronan, proteoglycans, and xenobiotic glucuronides. High levels of hyaluronan turnover in prostate cancer are correlated with aggressive progression. UGDH expression is high in the normal prostate even though hyaluronan accumulation is virtually undetectable. The enzyme's common role in the prostate may be to provide precursors for glucuronosyltransferase enzymes, which inactivate and solubilize androgens by glucuronidation. Androgen dependence of UGDH, glucuronosyltransferase, and hyaluronan synthase expression, overview
physiological function
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enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex. The hysteresis may be the consequence of a functional adaptation, by slowing the response of the enzyme to sudden increases in the flux of substrate, the other biochemical pathways that use this important metabolite will have a competitive edge
physiological function
precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
physiological function
precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
physiological function
-
the enzyme is involved in protein N-glycosylation
physiological function
the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
physiological function
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UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview. UDP-glucuronic acid is a key precursor for the synthesis of the glycosaminoglycan chain in proteoglycans
physiological function
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
physiological function
the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan
physiological function
the enzme synthesize UDP-glucuronate, a key sugar nucleotide involved in biosynthesis of the plant cell wall, the LgUGDH gene plays a role in controlling the biosynthesis of secondary cell walls
physiological function
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in Escherichia coli K-12, Ugd is important for biosynthesis of the environmentally regulated exopolysaccharide known as colanic acid, whereas in other Escherichia coli isolates, the same enzyme is required for production of the constitutive group 1 capsular polysaccharides, which act as virulence determinants; in Escherichia coli serotype K30, the enzyme is required for production of the constitutive group 1 capsular polysaccharides, which act as virulence determinants
physiological function
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UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces
physiological function
enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene
physiological function
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enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
physiological function
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enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene
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physiological function
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enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
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physiological function
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the enzyme is involved in protein N-glycosylation
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physiological function
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UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
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physiological function
-
the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan; UDP-glucose dehydrogenase is responsible for the NAD-dependent twofold oxidation of UDP-glucose to UDP-glucuronic acid, one of the key components for gellan biosynthesis
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physiological function
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the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
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physiological function
-
precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
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physiological function
Streptococcus pyogenes M1 GAS 5448
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precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
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additional information
mutation in either ugd leads to activation of RpoE, an extracytoplasmic function sigma factor that is activated by protein misfolding and alterations in cell surface structure in other bacteria. Activation of RpoE or RpoE overexpression causes inhibition of FlhDC and hemolysin expression
additional information
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mutation in either ugd leads to activation of RpoE, an extracytoplasmic function sigma factor that is activated by protein misfolding and alterations in cell surface structure in other bacteria. Activation of RpoE or RpoE overexpression causes inhibition of FlhDC and hemolysin expression
additional information
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dysregulated expression of UGDH can promote the development of androgen independent tumor cell growth by increasing available levels of intracellular androgen. UGDH activity is the rate limiting factor in solubilization of excess androgen from prostate tumor cells, overview
additional information
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the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
additional information
the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
additional information
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enzyme Ugd from Escherichia coli K-12 can functionally replace enzyme Ugd from Escherichia coli serotype K30 in biosynthesis of K30 capsular polysaccharide
additional information
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surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
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Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
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surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
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additional information
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Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
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additional information
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the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP-glucose + NAD+
CTP-glucuronate + NADH
Saccharum spp.
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8% of activity with UDP-glucose
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ir
dTDP-glucose + NAD+ + H2O
dTDP-glucuronate + NADH
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reaction rate is 16.7% of that with UDPglucose
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-
?
TDP-glucose + NAD+
TDP-glucuronate + NADH
Saccharum spp.
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2% of activity with UDP-glucose
-
-
ir
UDP-glucose + 3-pyridinealdehyde adenine dinucleotide
UDP-glucuronate
-
-
-
-
?
UDP-glucose + nicotinamide hypoxanthine dinucleotide + H2O
UDP-glucuronate + ?
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-
-
-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
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reaction rate is 5.5% of that with UDP-glucose
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-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
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17% of the reaction rate with UDP-glucose
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?
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
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reaction rate is 17% of that with UDPglucose
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-
?
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
38.5% of the rate with UDP-glucose
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
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-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
UDP-glucuronic acid is a key precursor in the biosynthesis of glycoconjugates
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?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is involved in protein N-glycosylation
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-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is involved in protein N-glycosylation
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-glucuronate is a key sugar nucleotide involved in biosynthesis of the plant cell wall
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
B5L017
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
B5L017
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
11.9% of the rate with UDP-glucose
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
6.4% of the rate with UDP-glucose
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
reversal of reaction cannot be demonstrated
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
recombinant forms Ugd(BCAL2946) and Ugd(BCAM0855) have similar in vitro Ugd activity
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
NADP+, about 1% of activity of NAD+
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
C276 is an active catalytic residue and critically involved in the substrate binding
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
the enzyme has dual specificity with UDP-glucose and ethanol
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
the enzyme has a crucial role during development of Xenopus laevis. Silencing of UGDH decreases glycosaminoglycan synthesis causing severe embryonic malformations because of defective gastrulation process
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
several different UDPGDH isoenzymes contribute to UDP-glucuronate and hence wall matrix biosynthesis in maize
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
UDPGDH-A activity has a more important role than UDPGDH-B in synthesis of UDP-glucuronate
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
-
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
-
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
35% of the rate with UDP-glucose
-
-
?
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
6.3% of the rate with UDP-glucose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
first step of a branched pathway leading to plant cell-wall polysaccharides which contain glucuronic and galacturonic acids and the pentoses xylose, arabinose and apiose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
additional information
?
-
-
importance of both UDPDH and mshA gene expression for successful light organ colonization in the sepiolid squid Euprymna tasmanica
-
-
-
additional information
?
-
-
no substrate: ADP-glucose, TDP-glucose
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
no activity with uridine diphosphoacetylgalactosamine
-
-
-
additional information
?
-
-
no activity with uridine diphosphoacetylglucosamine
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
-
additional information
?
-
-
no substrates: UDP-D-galactose, UTP, 5'-UMP and D-galactose
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with: 3-pyridinealdehyde deamino adenosine dinucleotide
-
-
-
additional information
?
-
-
no substrate: UDP-galactose, UDP-N-galactosamin, ADP-glucose, GDP-glucose, GDP-mannose
-
-
-
additional information
?
-
-
enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex
-
-
-
additional information
?
-
-
the transient capacity to dissociate and reorganize the hydrogen bond network at the interface between dimeric units is an important element of the normal catalytic cycle
-
-
-
additional information
?
-
-
no reaction with ethylnicotinate adenine dinucleotide
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with 3-formylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with 3-propionylpyridine adenine dinucleotide
-
-
-
additional information
?
-
the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
-
-
-
additional information
?
-
the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the transient capacity to dissociate and reorganize the hydrogen bond network at the interface between dimeric units is an important element of the normal catalytic cycle
-
-
-
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
UDP-glucuronic acid is a key precursor in the biosynthesis of glycoconjugates
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
Q9HQQ9
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
Q9HQQ9
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
D4GYH5
the enzyme is involved in protein N-glycosylation
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
D4GYH5
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
D4GYH5
the enzyme is involved in protein N-glycosylation
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
A0A0E4FJQ1
-
UDP-glucuronate is a key sugar nucleotide involved in biosynthesis of the plant cell wall
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
O70199
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
O70199
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
A4UTT2
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
A4UTT2
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
W0A856
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
W0A856
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
Q56R95
the enzyme has a crucial role during development of Xenopus laevis. Silencing of UGDH decreases glycosaminoglycan synthesis causing severe embryonic malformations because of defective gastrulation process
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
several different UDPGDH isoenzymes contribute to UDP-glucuronate and hence wall matrix biosynthesis in maize
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
UDPGDH-A activity has a more important role than UDPGDH-B in synthesis of UDP-glucuronate
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
C3VI43
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
A4UTT2
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
A4UTT2
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
first step of a branched pathway leading to plant cell-wall polysaccharides which contain glucuronic and galacturonic acids and the pentoses xylose, arabinose and apiose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
cofactor binding triggers the formation of the 32 symmetry enzyme hexamer, which is the catalytically relevant state
additional information
-
no constantly bound chromophoric cofactors, i.e. NAD+, required
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
additional information
NaCl
-
is able to function in a variety of salt concentrations, enzymatic activity improves as salinity decreases. At 4 M NaCl concentration the enzyme was able to produce 870 nM NADH, while at 0.5 M NaCl, over 1.5 mM NADH is produced
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
gallic acid
-
is a non-competitive inhibitor with respect to UDP-glucose and NAD+. It decreases specific activities of UGDH, but does not affect UGDH protein expression, thus UGDH activity is inhibited by polyphenols at the post-translational level. Gallic acid exerts strong antiproliferative activity in breast cancer cells. Heat inactivation of UGDH is accelerated to a greater degree by quercetin than by gallic acid. In the presence of gallic acid, the activity remaining after 30 min is 55% that of control
NaCl
VNG1048G loses much of its activity when salinity drops below 3 M NaCl
NAD+
-
substrate inhibition, reversible by the addition of a nucleotide triphosphate, e.g. ATP, in the absence of kinase. Mutations in a previously identified UDP-glucuronic acid allosteric binding site decrease the binding affinity of the nucleotide triphosphate
quercetin
-
shows a competitive inhibition and a mixed-type inhibition with respect to UDP-glucose and NAD+, decreases specific activities of UGDH, but does not affect UGDH protein expression, thus UGDH activity is inhibited by polyphenols at the post-translational level. Quercetin exerts strong antiproliferative activity in breast cancer cells. Heat inactivation of UGDH is accelerated to a greater degree by quercetin than by gallic acid. In the presence of quercetin, the activity remaining after 30 min is 20% that of control
UDP-alpha-D-xylose
-
competitive. The DELTA132 deletion mutant and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces, suggesting that the hinge-bending motion represents a path for the allosteric transition between the different hexameric states
UDP-glucuronic acid
product inhibition, 44% residual activity at 1 mM; product inhibition, 79% residual activity at 1 mM
Uridine 5'-diphosphate chloroacetol
-
alkylates a thiol group of cysteine in the catalytic centre via being specifically bound instead of the substrate
NADH
-
0.1 mM, presence of 0.1 mM NAD+, 44% inhibition, presence of 0.5 mM NAD+, 6% inhibition
NADH
product inhibition, 26% residual activity at 0.05 mM; product inhibition, 70% residual activity at 0.05 mM
piperine
-
stronger inhibition with intestinal cell enzyme than with rat liver enzyme
piperine
-
non-competitive, reversible, non-pH-dependent, 90% inhibition at concentration 0.05 mM and 10% inhibition at concentration 0.01 mM
UDP-xylose
-
allosteric feedback inhibitor, reduces significantly the activity of the enzyme
additional information
-
the enzyme from serotype K30 is not inhibited by NAD+, in contrast to Escherichia coli K-12
-
additional information
-
no substrate inhibition, K+ is not inhibitory up to 500 mM, not inhibitory: dimethyldicarbonate, EDTA
-
additional information
-
in the presence of 0.12 mM 5-azido-UDP-glucose, 89% of the enzyme activity is lost after 5 min of photolabeling. When the enzyme is photolyzed in presence of 1 mM UDP-glucose, 11% of the enzyme activity is lost. 5-azido-UDP-glucose is photoinserting into a UDP-glucose-binding site on the human enzyme in a specific manner. Uracil, uridine, and glucose have a poor protective effect on the labeling, while UDP and UDP-glucose strongly inhibit photoinsertion
-
additional information
-
inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17beta-estradiol
-
upregulation of UDP-glucose dehydrogenase at mRNA, protein and activity level in articular chondrocyte
lactose
-
UDP-GlcDH activities in extracts of Lactococcus lactis strain NFHA01 induced with both 0.5% and 2% lactose are significantly higher than that of the same strain without induction. UDP-GlcDH activity of NFHA01 induced with 2% lactose is about 110% higher than that of 0.5% lactose induction
nisin
-
induces the expression of szHasA together with szHasB
additional information
-
the enzyme shows a mechanism of activation that is NTP-dependent, poor activation by UDP-alpha-D-glucose. The inclusion of MgCl2 in the reaction buffer reverses the NTP-dependent activation of UgdK-12, in a concentration-dependent manner. This is not specific to Mg2+ as a similar effect is found for other divalent cations, including Ca2+, Mn2+, Zn2+, and Ni2+. Monovalent cations do not affect UgdK-12 activity. Chelating the divalent cation with EDTA or EGTA restores the NTP-dependent activation of UgdK-12
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35 - 0.62
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, from different strains; pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP
0.034
UDP-alpha-D-glucose
-
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.23
UDP-alpha-D-glucose
wild-type, pH 8.7, 30°C, Hill-coefficient 0.89
additional information
additional information
-
KM increase at pH higher than 9.0
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetic, cooperative kinetic behavior occurs in the hexameric enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4 - 7.1
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, from different strains
56.2
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000143
purified dodecameric enzyme, pH 9.2, temperature not specified in the publication
additional information
additional information
-
14.0, 1 unit is defined as the amount of enzyme required to produce 0.0002 mM of NADH per min at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6
8.7
9.2
9.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
half-maximal activity at about pH 7.0 and pH 9.5, maximal activity at pH 8.0
9.5 - 11
-
pH 9.5: about 40% of maximal activity, pH 11.0: about 10% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
purified recombinant His-tagged enzyme, activity range, profile overview
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
silencing of UGDH decreases glycosaminoglycan synthesis causing severe embryonic malformations because of defective gastrulation process. Overexpression of the enzyme from Xenopus laevis in human smooth muscle cells increases the accumulation of hyaluronan
the abundance of enzyme mRNA in pistils is more than 3fold greater than that in other parts, and the abundance in stamens and calyx tubes is relatively high compared with that in sepals and petals
changes in the mRNA level during peach fruit development correspond to changes in the amount of cell wall material and the cell wall uronic acid content. These are greater in the fruits of the commercial cultivars compared with the Japanese native peach cultivars, and the expression of enzyme is higher in the fruits of the commercial cultivars
-
increased UGDH expression in cancerous acini and decreased expression in normal-appearing acini of the same prostate relative to acini of non-cancerous prostates
enzyme activity increases dramatically in a special subset of vulval cells during vulval morphogenesis
-
siRNA for the human enzyme is put into a pRNA-U6.1/Neo vector and chemically transfected into bresat cancer cells. The UGDH siRNA plasmid then knocks down UGDH expression in ZR-75-1 cells
additional information
-
overexpression of c-Krox in articular chondrocytes depresses both UDPGD mRNA steady-state level and protein expression
the level of mRNA in immature leaves is much higher than that in mature leaves
additional information
-
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
additional information
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
additional information
-
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
-
additional information
-
the organism grows optimally in 1.7-2.5 M NaCl
-
additional information
the LgUGDH gene is expressed in all larch plant organs, primarily in the larch stems, in addition to its roots and leaves
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Q7MVC7
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
47000
48500
50000
52000
57000
300000
340000
550000
52000
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
hexamer
homodimer
recombinant form of Ugd(BCAL2946); recombinant form of Ugd(BCAM0855)
monomer
tetramer
additional information
?
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
?
-
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
-
hexamer
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
additional information
-
structural modelling of the enzyme in complex with NAD and uridine 5'-monophosphate, using structure of Ugd from Klebsiella pneumoniae in complex with UDPGA, PDB ID 3PJG, as template
additional information
-
the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
-
the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
-
additional information
-
sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
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sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
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additional information
significant amount of dimeric and monomeric species can be detected
additional information
identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
additional information
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examination of the dimer-dimer subunit interface reveals an extensive network of charge interactions and hydrogen bonding that coordinately stabilize the hexamer in the presence and absence of its cofactor or substrate, involving residue T325. The wild-type UGDH enzyme purifies in a hexamer-dimer equilibrium and transiently undergoes dynamic motion that exposes the dimer-dimer interface during catalysis. Only dynamic UGDH hexamers support robust cellular function, mutant dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. Molecular interactions at the subunit interface, overview. In the apo form Thr325 directly forms a hydrogen bond with Asp105 of the opposite subunit
additional information
the Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
additional information
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the Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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possible role of Ugd phosphorylation in the production of a constitutively expressed capsular polysaccharide, no role for phosphorylation in modulating activity of Ugd. Escherichia coli might contain two bacterial tyrosine kinases, analysis of kinase deletion mutants of Escherichia coli strains, overview; tyrosine phosphorylation in the activation of Ugd of Escherichia coli K12. Possible role of Ugd phosphorylation in the production of a constitutively expressed capsular polysaccharide (CPS), no role for phosphorylation in modulating activity of Ugd. Escherichia coli might contain two bacterial tyrosine kinases, analysis of kinase deletion mutants of Escherichia coli strains, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged BceC, 0.001 ml of protein solution containing 5 mg/ml protein in 25 mM Tris-HCl, pH 8.3, 50 mM NaCl, 2.5 mM DTT, 0.25 mM UDP-GlcA, and 0.5 mM NAD+, is mixed with 0.001 ml of precipitant solution containing 200 mM ammonium sulfate, 100 mM sodium acetate, pH 4.5, 11% w/v PEG 4000, and 50 mM NaF, method optimiization, X-ray diffraction structure determination and analysis at 2.09 A resolution, molecular replacement
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2.3 A resolution crystal structure of the deletion construct DELTA132 reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the deletion construct as a hexamer with point group symmetry 32, similar to that of the active complex. In contrast, the UDP-alpha-D-xylose-inhibited enzyme forms a lower-symmetry, horseshoe-shaped hexameric complex. The DELTA132 and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
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alternate crystal structure of human enzyme in complex with UDP-glucose at 2.8 A resolution. The substrate-bound protein complex consists of the open homohexamer. In all subunits of the open structure, residue Thr131 has translocated into the active site occupying the volume vacated by the absent active water and partially disordered NAD+ molecule. This conformation suggests a mechanism by which the enzyme may exchange NADH for NAD+ and repolarize the catalytic water molecule bound to Asp280 while protecting the reaction intermediates
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crystallized from a solution of 0.2 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, and 21% PEG 8000. Diffraction data are collected to a resolution of 2.8 A. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 173.25, b = 191.16, c = 225.94 A and alpha = beta = gamma = 90.0°
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in mutant E161Q, the hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of mutant E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate. Residue Cys276 is covalently modified in the structure, establishing its role as catalytic nucleophile of the reaction
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mutant K94E, to 2.08 A resolution. Cofactor binding triggers the formation of the 32 symmetry hexamer, but substrate UDP-alpha-D-glucose is needed for the stability of the complex. Loop88-110 is the cofactor-responsive allosteric switch that drives hexamer formation, loop88-110 directly links cofactor binding to the stability of the hexamer-building interface. In the interface, loop88-110 packs against the Thr131-loop/alpha6 helix, the allosteric switch that responds to the feedback inhibitor UDP-alpha-D-xylose
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the structure of UGDH in the crystal form reveals a hexameric arrangement, composed a trimer of dimers of six subunits
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sitting-drop vapour-diffusion method, diffraction quality crystals (maximum dimensions of 0.1 * 0.1 * 0.1 mm) are obtained within one week at 273°C using reservoir solution composed of 4.0 M NaCl, 100 mM HEPES pH 7.5. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 117.7, b = 76.7, c = 75.6 A, beta = 125.8°. Crystal structure is at a resolution of 2.0 A. The overall fold is comprised of an N-terminal NAD+ dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long alpha-helix
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purified recombinant wild-type and selenomethionine-labeled UgdG at 4.5 and 5.5 mg/ml, respectively, in 25 mM Tris-HCl, pH 8.3, 50 mM NaCl, 2.5 mM DTT and 1 mM NAD+, or 0.5 mM UDP-GlcA and 1 mM NAD+, 0.0005 ml of each protein and precipitant solution are mixed at 20°C, 24 h, the precipitant solution contains 200 mM Li2SO4, 100 mM Tris-HCl, pH 8.5, and 30% v/v PEG 4000, or 100 mM sodium citrate, pH 5.6, 20% 2-propanol, and 20% v/v PEG 4000, vapour diffusion method, method optimization, X-ray diffraction structure determination and analysis at 2.4 A resolution for the wild-type enzyme, and at 3.4 A resolution for the SeMet-UDG
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
the purified recombinant His-tagged enzyme is stable from 15°C to 30°C retaining more than 60% of its residual activity, while it retains only 28% activity at 50°C
additional information
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thermal stabilities of wild-type and mutant enzymes, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable during repeated freezing and thawing cycles with 10% glycerol
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the half-life of UGDH catalytic activity in vitro is reduced by mutations at the dimer interface
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5°C, 50 mM Tris-HCl, pH 8.7, 2 mM dithiothreitol, after 24 h 90% activity left
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel affinity and gel filtration; by nickel affinity and gel filtration; by nickel affinity and gel filtration
partial
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography
recombinant His6-tagged BceC from Escherichia coli by affinity chromatography
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography to over 95% purity
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged UGDH from Escherichia coli by nickel affinity chromatography
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recombinant His6-tagged wild-type and selenomethionine-labeled UgdG from Escherichia coli BL21 and B843, respectively by affinity chromatography
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta2(DE3)pLysS by nickel affinity chromatography and dialysis
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recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
gene aglM, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme
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gene bceC, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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gene udg1, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme
gene Ugd(BCAL2946) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAL2946) expressed in Escherichia coli HMS 174(DE3); gene Ugd(BCAM0855) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAM0855) expressed in Escherichia coli HMS 174(DE3); gene Ugd(BCAM2034) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAM2034) expressed in Escherichia coli BL21 (DE3)
gene ugd, located near the colanic acid/group 1 CPS locus, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain CWG876; gene ugd, located near the colanic acid/group 1 CPS locus, recombinant overexpression of His6-tagged full-length enzyme and truncated enzyme comprising residues 447-704 in Escherichia coli strain CWG876
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gene ugdG, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH6alpha
gene ugdG, expression of His6-tagged wild-type and selenomethionine-labeled UgdG in Escherichia coli BL21 and B843, respectively
gene UgdG, overexpression of His6-tagged enzyme in Escherichia coli
gene UGDH, real-time quantitative PCR enzyme expression analysis
genes szHasA (hyaluronan synthase gene) and szHasB (UDP-glucose-6-dehydrogenase gene) introduced into Lactococcus lactis strain NZ9000 under the control of nisA promoter and lacA promoter respectively, resulting in a dual-plasmid controlled expression system
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hUGDH gene is cloned from a LNCaP cDNA library, from LNCaP C33 and C81 cells, expression of His6-tagged UGDH in Escherichia coli, expression of UGDH mutant D280N in HEK.293 cells
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overexpression as glutathione-S-transferase fusion protein in Escherichia coli
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overexpression of the enzyme from Xenopus laevis in human smooth muscle cells increases the accumulation of hyaluronan
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta2(DE3)pLysS, recombinant expression in HEK293 cells
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the enzyme UGDH is encoded by two paralogous genes, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, cloning in a plasmid with the CaMV 35S promoter, the GUS gene, and the nopaline synthase terminator, recombinant overexpression of UDP-glucose dehydrogenase from Larix gmelinii in Arabidopsis thaliana enhancing the content of soluble sugars and hemicelluloses and growth and cold tolerance in the transgenic plants, transfection via Agrobacterium tumefaciens strain LBA4404, realtime and reverse transcriptase PCR expression analysis. The transgenic plants show distinct phenotypes at different developmental stages, as compared to the wild-type, overview