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evolution
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the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
evolution
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UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure
evolution
bifunctional UDP-glucose 4-epimerases, UGEs, with UDP-xylose 4-epimerase (EC 5.1.3.5) activity are conserved in vascular plants
evolution
presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
evolution
sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
evolution
the rice genome contains four putative UGE-encoding genes (OsUGE1-4). All four predicted OsUGEs in rice carry an epimerase domain and belong to the NAD+ dependent epimerase/dehydratase family proteins that use NAD+ as a cofactor and nucleotide-sugars as substrates. Expression profiles of UGEs in Oryza sativa support distinct in planta roles throughout development
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)
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)
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)
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)
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)
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)
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). Despite the relatively low sequence identity among all three groups, the similarity of the enzymes' tertiary structures is striking with an overall RMSD of the multiple structure alignment being 1.08 A and variation being most pronounced at the C-terminal end
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. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
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 group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
evolution
the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
evolution
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the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
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evolution
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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)
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evolution
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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)
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evolution
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sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
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evolution
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the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
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evolution
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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. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
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evolution
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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 group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
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evolution
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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)
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evolution
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presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
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malfunction
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GALE deficiency leads to mild or severe disease with clinical symptoms similar to classical galactosemia
malfunction
UDP-galactose-4-epimerase deficiency causes galactosemia. Altered protein stability is due to misfolding and loss or reduction of enzyme activity is responsible for the molecular defects underlying GALE-deficiency galactosemia
malfunction
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a Xcc galE mutant has reduced biofilm formation ability
malfunction
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In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
malfunction
enzyme overexpressing mutant OsUGE1-OX lines maintain 18-24% more sucrose and 12-22% less cellulose in shoots compared to wild-type when subjected to suboptimal N-levels. OsUGE1-OX lines maintain proportionally more galactose and glucose in the hemicellulosic polysaccharide profile of plants compared to wild-type plants when grown under low N. The altered cell wall C-partitioning during N-limitation in the OsUGE1-OX lines appears to be mediated by OsUGE1 via the repression of the cellulose synthesis associated genes, OsSus1, OsCesA4, 7, and 9. OsUGE1 shows phenotypic alteration at carbohydrate partitioning level in the transgenic lines, overexpressinon phenotypes, overview
malfunction
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
malfunction
mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
malfunction
mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
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 replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
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
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identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
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malfunction
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mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
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malfunction
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a Xcc galE mutant has reduced biofilm formation ability
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malfunction
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In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
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malfunction
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the replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
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malfunction
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mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
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metabolism
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GALE catalyzes the third step of the Leloir pathway of galactose metabolism
metabolism
GALE is involved in the galactose metabolic pathway
metabolism
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UgeA interconverts UDP-glucose and UDP-galactose and participates in galactose metabolism
metabolism
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overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
metabolism
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the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
metabolism
the enzyme is involved in D-galactose metabolism
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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metabolism
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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metabolism
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the enzyme is involved in D-galactose metabolism
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metabolism
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the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
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metabolism
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overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
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metabolism
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the enzyme is involved in D-galactose metabolism
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metabolism
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
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enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis, gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
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galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
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galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
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GalE plays a key role in lipopolysaccharide biosynthesis
physiological function
the enzyme induces moderate protection against challenge infection
physiological function
the enzyme produces the precursor UDP-galactopyranose required for galactofuranose synthesis
physiological function
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UDP-Gal provides all galactosyl units in biologically synthesized carbohydrates. All healthy cells produce UDP-Gal from uridine 5'-diphospho-alpha-D-glucose UDP-Glc, by the action of UDP-galactose 4-epimerase
physiological function
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Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
physiological function
enzyme OsUGE1 plays an important role in carbohydrate partitioning to the cell wall in Oryza sativa
physiological function
enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UGE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UGE is important in the composition of the sugar nucleotide pools
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UXE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UXE is important in the composition of the sugar nucleotide pools
physiological function
UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
physiological function
UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
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, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
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 is important for the biosynthesis of other polysaccharide structures, such as capsular polysaccharide (CPS), or extracellular polysaccharide (EPS) from Streptococcus thermophilus, one of the most widely used bacteria in the dairy industry
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of other polysaccharide structures, such as proteoglycans (PGs) of articular chondrocytes. Secondary role of the human enzyme is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc)
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures, such as capsular polysaccharide (CPS)
physiological function
UDP-galactose 4-epimerase plays an essential role in development and homeostasis of Drosophila that extends beyond the Leloir pathway. UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
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
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UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
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physiological function
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UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
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physiological function
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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
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physiological function
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UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
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physiological function
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UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
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physiological function
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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, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
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physiological function
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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
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physiological function
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Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
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physiological function
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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
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physiological function
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UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
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physiological function
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enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
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homology structural modeling, overview
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ligand binding structures, docking study, overview
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ligand binding structures, docking study, overview
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ligand-bound enzyme structures, active site structure including Lys153, Tyr149, and Ser124, overview
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putative GalE catalytic residues are Ser124, Tyr147, and Lys151
additional information
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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
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comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
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comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
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comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
additional information
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comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
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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
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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
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enzyme structure and substrate specificity, structure-function relationship, overview. Comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes
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Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
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the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
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the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
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the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
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comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
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additional information
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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
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additional information
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Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
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additional information
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putative GalE catalytic residues are Ser124, Tyr147, and Lys151
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additional information
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the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
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additional information
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homology structural modeling, overview
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additional information
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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
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additional information
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comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
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