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UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-D-glucose
UDP-D-galactose
UDP-glucose
UDP-galactose
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
-
-
-
r
additional information
?
-
UDP-D-glucose
UDP-D-galactose
-
-
-
-
r
UDP-D-glucose
UDP-D-galactose
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
-
r
UDP-D-glucose
UDP-D-galactose
-
the achieved reasonable conversion rates the amount of enzyme used is increased 200fold comparted to UDP-N-acetyl-D-glucosamine as substrate. Substrate conversions reach 20% for UDP-Glc and 65% for UDP-Gal
-
r
UDP-D-glucose
UDP-D-galactose
-
unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-Glc and UDP-Gal than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine
-
-
r
UDP-GlcNAc
UDP-GalNAc
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
equilibrium reaction resulting in a 70:30 ratio of UDP-GlcNAc to UDP-GalNAc, irrespective of the initial substrate
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
wild-type enzyme is more efficient in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine than in catalyzing the epimerization of UDP-glucose and UDP-galactose
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
Q81JK4
-
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
-
-
r
additional information
?
-
Q81JK4
the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
-
the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
-
the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors
-
-
?
additional information
?
-
substrate specificity of KfoA, overview. KfoA epimerizes both acetylated and non-acetylated (UDP-Glc) substrates, EC 5.1.3.2, but its kcat/Km value for UDP-GlcNAc is approximately 1300fold that for UDP-Glc. Recombinant KfoA showes a strong preference for acetylated substrates in vitro. Coupling of K4 chondroitin polymerase (KfoC) and KfoA to determine the activity of UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
substrate specificity of KfoA, overview. KfoA epimerizes both acetylated and non-acetylated (UDP-Glc) substrates, EC 5.1.3.2, but its kcat/Km value for UDP-GlcNAc is approximately 1300fold that for UDP-Glc. Recombinant KfoA showes a strong preference for acetylated substrates in vitro. Coupling of K4 chondroitin polymerase (KfoC) and KfoA to determine the activity of UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
-
the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2
-
-
?
additional information
?
-
-
UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
-
-
?
additional information
?
-
-
the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
-
-
?
additional information
?
-
the group 3 epimerase WbpP from Pseudomonas aeruginosa is very specific for N-acetylated substrates
-
-
?
additional information
?
-
-
enzyme regulates gastric mucous aminosugar metabolism
-
-
?
additional information
?
-
two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
-
-
?
additional information
?
-
two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
-
-
?
additional information
?
-
enzyme TMGalE also has high activity for epimerization of UDP-Gal to UDP-Glc, EC 5.1.3.2. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively
-
-
?
additional information
?
-
-
Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-D-glucose
UDP-D-galactose
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
-
-
-
r
additional information
?
-
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20
-
?
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
Q81JK4
-
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
-
-
r
additional information
?
-
Q81JK4
the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
-
the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
-
-
?
additional information
?
-
-
the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors
-
-
?
additional information
?
-
-
UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
-
-
?
additional information
?
-
-
the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
-
-
?
additional information
?
-
-
enzyme regulates gastric mucous aminosugar metabolism
-
-
?
additional information
?
-
-
Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 3
evolution
KfoA shows a high degree of identity with members of GalE group 2
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa). The enzyme from Pleisomonas shigelloides is a group 3 epimerase. The model of the '297-308 belt' is proposed to determine substrate specificity in group 3 members. The belts conformation supports (i) the formation of a hydrophobic cluster that interacts with the methyl group of the N-acetyl moiety, (ii) a correct positioning of the Asn195, and (iii) orients the substrate so the GlcNAc moiety will form hydrogen bonds with Ser143 and Ser144. Due to this belt and the resulting hydrogen bond network, the group 3 members have a distinct conformation at this region whereas the conformation of group 1 and group 2 enzymes is very similar
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa). The model of the '297-308 belt' is proposed to determine substrate specificity in group 3 members. The belts conformation supports (i) the formation of a hydrophobic cluster that interacts with the methyl group of the N-acetyl moiety, (ii) a correct positioning of the Asn195, and (iii) orients the substrate so the GlcNAc moiety will form hydrogen bonds with Ser143 and Ser144. Due to this belt and the resulting hydrogen bond network, the group 3 members have a distinct conformation at this region whereas the conformation of group 1 and group 2 enzymes is very similar
evolution
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group 2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
evolution
-
KfoA shows a high degree of identity with members of GalE group 2
-
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
-
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
-
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
-
evolution
-
Gne epimerases, excluding enzymes active on UDP-N-acetylgalactosaminuronic acid and undecaprenyl diphosphate-N-acetylgalactosamine, named GnaB or Gnu, are in the same clade as the GalE 4-epimerases for interconversion of UDP-glucose and UDP-galactose, phylogenetic analysis, overview
-
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group 2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
-
malfunction
silencing GALE gene with specific siRNAs results in a markedly inhibition of proteoglycans (PGs)synthesis in human articular chondrocytes. GALE protein levels are also decreased in both human osteoarthritis cartilage, thus leading to losses of PGs contents. GALE inhibition might contribute to osteoarthritis progress. Mutations of gene GALE in humans results in an inherited metabolic disease, the type III galactosemia
malfunction
the S306Y mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
malfunction
the S306Y mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates,which results in the observed loss of activity
metabolism
the enzyme is involved in biosynthetic pathway of the glycan 2-deoxy-L-altruronic acid that is found in the lipopolysaccharide of Pleisomonas shigelloides
metabolism
the enzyme is involved in D-galactose metabolism
metabolism
-
the enzyme is involved in biosynthetic pathway of the glycan 2-deoxy-L-altruronic acid that is found in the lipopolysaccharide of Pleisomonas shigelloides
-
metabolism
-
the enzyme is involved in D-galactose metabolism
-
metabolism
-
the enzyme is involved in D-galactose metabolism
-
physiological function
-
gene is important to biofilm formation because of its involvement in epimerizing UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
Q81JK4
the epimerase is required to produce N-acetyl-galactosamine for BclA oligosaccharide biosynthesis, a collagen-like glycoprotein, UDP-GlcNAc 4-epimerase encoded by the BAS5304 gene is required for the synthesis of GalNAc in sporulating cells and that GlcNAc can replace GalNAc in the synthesis of BclA oligosaccharides
physiological function
KfoA, encoded by a gene from region 2 of the K4 capsular gene cluster, shows high homology to the UDP-glucose-4-epimerase (GalE) from Escherichia coli. KfoA is reputed to be responsible for uridine 5'-diphosphate-N-acetylgalactosamine (UDP-GalNAc) supply for K4CP biosynthesis in vivo. KfoA is a higher efficiency UDP-GalNAc provider than GalE, supported by a coupled assay developed based on the donor-acceptor combination specificity of Escherichia coli K4 chondroitin polymerase (KfoC). KfoA has a higher affinity for UDP-GlcNAc than GalE, EC 5.1.3.2
physiological function
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
physiological function
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
physiological function
UDP-galactose-4-epimerase (GALE) is a key enzyme catalyzing the interconversion of UDP-glucose and UDP-galactose, as well as UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine, which are all precursors for the proteoglycans (PGs) synthesis. Role of GALE in PGs synthesis of human articular chondrocytes, the GALE expression in osteoarthritis, and the regulation of GALE expression by interleukin-1beta, overview. GALE mRNA expression is stimulated by interleukin-1beta in early phase, but suppressed in late phase, while the suppression of GALE expression induced by interleukin-1beta is mainly mediated by stress-activated protein kinase/c-Jun N-terminal kinase pathway. Both SAP/JNK inhibitor SP600125 and p38 MAPK inhibitor SB203580 attenuate the suppression of interleukin-1beta on GAG synthesis and GALE mRNA expression of chondrocyte. Critical role of GALE in maintaining cartilage homeostasis
physiological function
-
KfoA, encoded by a gene from region 2 of the K4 capsular gene cluster, shows high homology to the UDP-glucose-4-epimerase (GalE) from Escherichia coli. KfoA is reputed to be responsible for uridine 5'-diphosphate-N-acetylgalactosamine (UDP-GalNAc) supply for K4CP biosynthesis in vivo. KfoA is a higher efficiency UDP-GalNAc provider than GalE, supported by a coupled assay developed based on the donor-acceptor combination specificity of Escherichia coli K4 chondroitin polymerase (KfoC). KfoA has a higher affinity for UDP-GlcNAc than GalE, EC 5.1.3.2
-
physiological function
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
physiological function
-
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
-
physiological function
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
additional information
-
modeling of specific substrate recognition by UDP-GalNAc 4-epimerases based on mutational analysis and structure, overview
additional information
-
structure homology modeling, overview. The Marinithermus enzyme makes use of a TxnYx3K catalytic triad rather than the usual SxnYx3K triad. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine, the gatekeeper residue is responsible for the substrate specificity, the two consecutive glycine residues, Gly118 and Gly119, are a unique feature of GalE enzymes from Thermus species and important for activity as well as affinity
additional information
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
additional information
enzyme structure and substrate specificity, comparison of the hexagonal box model of sugar-binding pockeets of several UDP-sugar 4-epimerases. Importance and flexibility of the hydrogen bond network
additional information
enzyme structure and substrate specificity, structure-function relationship, overview. Comparison of the hexagonal box model of sugar-binding pockeets of several UDP-sugar 4-epimerases. Importance and flexibility of the hydrogen bond network. Structural characterization of WbpP in the presence of both substrates, modeling of the substrate-binding pocket represented as a hexagonal-shaped box with the bottom formed by the nicotinamide ring of the cofactor and an open top to accommodate the ring-flipping movement during catalysis. Three of the six walls of the hexagonal box are formed by highly conserved residues: Ser142, Tyr166 and Asn195 in WbpP. The other three walls (Gly102, Ala209 and Ser306 for WbpP) have been proposed to be key determinants for substrate specificity, overview. The so-called gatekeeper wall is occupied by a bulky residue (Tyr299) in Escherichia coli GalE, which is unable to catalyse the epimerization of acetylated substrates, whereas enzymes with a smaller residue are able to convert acetylated substrates
additional information
residue Ser301, located near the UDP-GlcNAc binding pocket, plays an important role in the determination of the conversion ratio of UDP-GlcNAc to UDP-GalNAc by KfoA. Structural modeling of KfoA constructed based on the crystal structure of human GalE (PDB ID 1HZJ), a model member of group 2. The model of KfoA contains the conserved motif necessary for enzymatic activity and one characteristic Rossmann fold scaffold sequence. The modified Rossmann fold of seven strands of parallel beta-sheet flanked on either side by alpha-helices is located in the N-terminal domain and is believed to be involved in cofactor binding. The C-terminal portion is composed of six beta-strands and five alpha-helices and involved in UDP-GlcNAc binding
additional information
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
-
residue Ser301, located near the UDP-GlcNAc binding pocket, plays an important role in the determination of the conversion ratio of UDP-GlcNAc to UDP-GalNAc by KfoA. Structural modeling of KfoA constructed based on the crystal structure of human GalE (PDB ID 1HZJ), a model member of group 2. The model of KfoA contains the conserved motif necessary for enzymatic activity and one characteristic Rossmann fold scaffold sequence. The modified Rossmann fold of seven strands of parallel beta-sheet flanked on either side by alpha-helices is located in the N-terminal domain and is believed to be involved in cofactor binding. The C-terminal portion is composed of six beta-strands and five alpha-helices and involved in UDP-GlcNAc binding
-
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H305A
-
site-directed mutagenesis, structure determination and analysis, the mutant shows reduced activity with UDP-N-acetylglucosamine
S144T/H305A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A/S306Y
-
site-directed mutagenesis, the mutant shows no activity with either UDP-GlcNAc or UDP-Glc
G118A/G119A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
G188S/G119S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S116A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S279Y
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
T117S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S306Y
site-directed mutagenesis, the mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
G102K/Q201E
site-directed mutagenesis, as a result of the introduction of both mutations at the same time, a salt bridge is formed, which results in a rescue of the activity for acetylated substrates, probably due to restoration of the slight distortion that is observed in both single mutants
Q201E/G102K
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine, no epimerization activity with UDP-D-glucose and very limited activity with UDP-D-galactose
S143A
-
mutant enzyme shows epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type enzyme and no epimerization activity with UDP-D-glucose and UDP-D-galactose
S144K
-
mutant enzyme shows no epimerization activity with UDP-N-acetyl-D-glucosamine/UDP-N-acetyl-D-galactosamine and UDP-D-glucose/UDP-D-galactose
C300Y
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
K86G
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
C300Y
-
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
-
K86G
-
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
-
S301Y
site-directed mutagenesis, the mutation in KfoA results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
S301Y
-
site-directed mutagenesis, the mutation in KfoA results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
-
A209H
-
mutant enzyme shows very limited epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and slightly reduced epimerization activity with UDP-D-glucose and UDP-D-galactose
A209H
-
unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-glucose and UDP-galactose than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine
A209H
site-directed mutagenesis, the mutation results in limited ability to epimerize acetylated residues
A209N
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and very limited epimerization activity with UDP-D-glucose and UDP-D-galactose
A209N
site-directed mutagenesis, the mutation enhances the specificity for acetylated substrates accompanied by a lower catalytic efficiency
G102K
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and no epimerization activity with UDP-D-glucose and UDP-D-galactose
G102K
site-directed mutagenesis, the mutation slightly reduces activity on acetylated substrates and almost abolishes activity on non-acetylated substrates
Q201E
-
mutant enzyme shows slightly epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type activity and very limited epimerization activity with UDP-D-Glc and UDP-D-Gal
Q201E
site-directed mutagenesis, the mutation slightly reduces activity on acetylated substrates and almost abolishes activity on non-acetylated substrates
S306Y
-
completely inactive mutant enzyme
S306Y
site-directed mutagenesis, the mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity. The S306Y mutation in WbpP totally abolishes the activity of the enzyme
additional information
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
a gne-deficient mutant completely lacks UDPGalNAc 4-epimerase activity and has UDP-Gal 4-epimerase activity in after growth on D-glucose or D-galactose that is not significantly different from that of the wild-type strain. Mutation increases the surface hydrophobicity, produces deep alterations in the outer membrane architecture, and results in noticeable increases in the sensitivity to microcidal peptides, to eel and human sera, and to phagocytosis/opsonophagocytosis. Significant attenuation of virulence for eels and mice is observed with the mutant
additional information
-
a gne-deficient mutant completely lacks UDPGalNAc 4-epimerase activity and has UDP-Gal 4-epimerase activity in after growth on D-glucose or D-galactose that is not significantly different from that of the wild-type strain. Mutation increases the surface hydrophobicity, produces deep alterations in the outer membrane architecture, and results in noticeable increases in the sensitivity to microcidal peptides, to eel and human sera, and to phagocytosis/opsonophagocytosis. Significant attenuation of virulence for eels and mice is observed with the mutant
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Nishikawa, J.; Iwawaki, H.; Takubo, Y.; Nishihara, T.; Kondo, M.
Appearance of uridine 5'-diphospho-N-acetylglucosamine-4-epimerase during sporulation of Bacillus megaterium
Microbiol. Immunol.
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1986
Priestia megaterium
brenda
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Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant
Cell
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Cricetulus griseus
brenda
Yamamoto, K.; Kondo, Y.; Kumagai, H.; Tochikura, T.
Purification and some properties of UDP-N-acetylglucosamine 4-epimerase from Bacillus subtilis
Agric. Biol. Chem.
49
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Bacillus subtilis
-
brenda
Piller, F.; Eckhardt, A.E.; Hill, R.L.
The preparation of UDP-N-acetylgalactosamine from UDP-N-acetylglucosamine employing UDP-N-acetylglucosamine-4-epimerase
Anal. Biochem.
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Sus scrofa
brenda
Yamamoto, K.; Kawai, H.; Tochikura, T.
Preparation of uridine diphosphate-N-acetylgalactosamine from uridine diphosphate-N-acetylglucosamine by using microbial enzymes
Appl. Environ. Microbiol.
41
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Bacillus subtilis
brenda
Glowacka, D.; Zwierz, K.; Gindzienski, A.; Galasinski, W.
The metabolism of UDP-N-acetyl-D-glucosamine in the human gastric mucous membrane. II. The activity of UDP-N-acetylglucosamine 4-epimerase (E.C. 5.1.3.7)
Biochem. Med.
19
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Homo sapiens
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Hiatt, W.R.; Whiteley, H.R.
Activity of uridine diphosphate N-acetylglucosamine-4-epimerase during spherulation of Physarum polycephalum
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118
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Physarum polycephalum
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UDP-N-acetyl-D-glucosamine 4-epimerase
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8
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Gallus gallus
-
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The biosynthesis of N-acetylgalactosamine
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Bacillus subtilis
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Genetic and biochemical characterization of Bacillus subtilis 168 mutants specifically blocked in the synthesis of the teichoic acid poly(3-O-beta-D-glucopyranosyl-N-acetylgalactosamine 1-phosphate): gneA, a new locus, is associated with UDP-N-acetylglucosamine 4-epimerase activity
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Bacillus subtilis
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Galactosamine-synthesizing enzymes are induced when Giardia encysts
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56
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Giardia intestinalis
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The gut in the acute response: changes in colonic and hepatic enzyme activity in response to dermal inflammation in the rat
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73
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Kosaka, N.; Tanaka, H.; Ishii, A.; Shuto, K.
Effect of 5-[2-(diethylamino)ethyl]amino-5,11-dihydro[1]benzoxepino[3,4-b]pyridine trihydrochloride (KW-5805) on the biosynthesis of rat gastric mucus
Nippon Yakurigaku Zasshi
104
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Rattus norvegicus
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Degeest, B.; Vaningelgem, F.; Laws, A.P.; De Vuyst, L.
UDP-N-acetylglucosamine 4-epimerase activity indicates the presence of N-acetylgalactosamine in exopolysaccharides of Streptococcus thermophilus strains
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67
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Streptococcus thermophilus
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Winans, K.A.; Bertozzi, C.R.
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to inhibit O-linked glycosylation
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Homo sapiens
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Creuzenet, C.; Belanger, M.; Wakarchuk, W.W.; Lam, J.S.
Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6
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Pseudomonas aeruginosa
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Demendi, M.; Ishiyama, N.; Lam, J.S.; Berghuis, A.M.; Creuzenet, C.
Towards a better understanding of the substrate specificity of the UDP-N-acetylglucosamine C4 epimerase WbpP
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389
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Pseudomonas aeruginosa
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Ishiyama, N.; Creuzenet, C.; Lam, J.S.; Berghuis, A.M.
Crystal structure of WbpP, a genuine UDP-N-acetylglucosamine 4-epimerase from Pseudomonas aeruginosa: substrate specificity in udp-hexose 4-epimerases
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Pseudomonas aeruginosa
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Bernatchez, S.; Szymanski, C.M.; Ishiyama, N.; Li, J.; Jarrell, H.C.; Lau, P.C.; Berghuis, A.M.; Young, N.M.; Wakarchuk, W.W.
A single bifunctional UDP-GlcNAc/Glc 4-epimerase supports the synthesis of three cell surface glycoconjugates in Campylobacter jejuni
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Campylobacter jejuni
brenda
Lopez, A.B.; Sener, K.; Trosien, J.; Jarroll, E.L.; van Keulen, H.
UDP-N-acetylglucosamine 4-epimerase from the intestinal protozoan Giardia intestinalis lacks UDP-glucose 4-epimerase activity
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54
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Giardia intestinalis (Q868I5), Giardia intestinalis
brenda
Valiente, E.; Jimenez, N.; Merino, S.; Tomas, J.M.; Amaro, C.
Vibrio vulnificus biotype 2 serovar E gne but not galE is essential for lipopolysaccharide biosynthesis and virulence
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76
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Vibrio vulnificus (Q7MH46), Vibrio vulnificus
brenda
Niou, Y.K.; Wu, W.L.; Lin, L.C.; Yu, M.S.; Shu, H.Y.; Yang, H.H.; Lin, G.H.
Role of galE on biofilm formation by Thermus spp.
Biochem. Biophys. Res. Commun.
390
313-318
2009
Thermus thermophilus
brenda
Dong, S.; Chesnokova, O.N.; Turnbough, C.L.; Pritchard, D.G.
Identification of the UDP-N-acetylglucosamine 4-epimerase involved in exosporium protein glycosylation in Bacillus anthracis
J. Bacteriol.
191
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2009
Bacillus anthracis (Q81JK4), Bacillus anthracis
brenda
Bhatt, V.S.; Guo, C.Y.; Guan, W.; Zhao, G.; Yi, W.; Liu, Z.J.; Wang, P.G.
Altered architecture of substrate binding region defines the unique specificity of UDP-GalNAc 4-epimerases
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20
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Plesiomonas shigelloides (Q7BJX9), Plesiomonas shigelloides O17 (Q7BJX9)
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Beerens, K.; Soetaert, W.; Desmet, T.
Characterization and mutational analysis of the UDP-Glc(NAc) 4-epimerase from Marinithermus hydrothermalis
Appl. Microbiol. Biotechnol.
97
7733-7740
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Marinithermus hydrothermalis
brenda
Bhatt, V.S.; Guan, W.; Xue, M.; Yuan, H.; Wang, P.G.
Insights into role of the hydrogen bond networks in substrate recognition by UDP-GalNAc 4-epimerases
Biochem. Biophys. Res. Commun.
412
232-237
2011
Escherichia coli
brenda
Cunneen, M.M.; Liu, B.; Wang, L.; Reeves, P.R.
Biosynthesis of UDP-GlcNAc, UndPP-GlcNAc and UDP-GlcNAcA involves three easily distinguished 4-epimerase enzymes, Gne, Gnu and GnaB
PLoS ONE
8
e67646
2013
Escherichia coli, Yersinia pseudotuberculosis, Yersinia enterocolitica, Escherichia coli O157, Yersinia enterocolitica O:8, Escherichia coli O86, Yersinia pseudotuberculosis O6 and O7
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Zhu, H.M.; Sun, B.; Li, Y.J.; Meng, D.H.; Zheng, S.; Wang, T.T.; Wang, F.S.; Sheng, J.Z.
KfoA, the UDP-glucose-4-epimerase of Escherichia coli strain O5 K4 H4, shows preference for acetylated substrates
Appl. Microbiol. Biotechnol.
102
751-761
2018
Escherichia coli (Q8L0V2), Escherichia coli ATCC 23502 / K4 (Q8L0V2)
brenda
Shin, S.; Choi, J.; Di Luccio, E.; Lee, Y.; Lee, S.; Lee, S.; Lee, S.; Lee, D.
The structural basis of substrate promiscuity in UDP-hexose 4-epimerase from the hyperthermophilic Eubacterium Thermotoga maritima
Arch. Biochem. Biophys.
585
39-51
2015
Thermotoga maritima (Q9WYX9), Thermotoga maritima DSM 3109 (Q9WYX9), Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 (Q9WYX9)
brenda
Wen, Y.; Qin, J.; Deng, Y.; Wang, H.; Magdalou, J.; Chen, L.
The critical role of UDP-galactose-4-epimerase in osteoarthritis modulating proteoglycans synthesis of the articular chondrocytes
Biochem. Biophys. Res. Commun.
452
906-911
2014
Homo sapiens (Q14376)
brenda
Chen, L.L.; Han, D.L.; Zhai, Y.F.; Wang, J.H.; Wang, Y.F.; Chen, M.
Characterization and mutational analysis of two UDP-galactose 4-epimerases in Streptococcus pneumoniae TIGR4
Biochemistry (Moscow)
83
37-44
2018
Streptococcus pneumoniae (A0A0H2URG4), Streptococcus pneumoniae ATCC BAA-334 / TIGR4 (A0A0H2URG4)
brenda
Beerens, K.; Soetaert, W.; Desmet, T.
UDP-hexose 4-epimerases a view on structure, mechanism and substrate specificity
Carbohydr. Res.
414
8-14
2015
Plesiomonas shigelloides (Q7BJX9), Pseudomonas aeruginosa (Q8KN66)
brenda
Dadashipour, M.; Iwamoto, M.; Hossain, M.M.; Akutsu, J.I.; Zhang, Z.; Kawarabayasi, Y.
Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii
J. Bacteriol.
200
e00048-18
2018
no activity in Sulfolobus tokodaii
brenda