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evolution
Archaea synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses
evolution
Q81TP1
structural comparison of the enzyme structure with RfbC homologues shows that the key active-site residues are conserved across kingdoms. RmlC-like epimerases belongs to the diverse cupin superfamily
evolution
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structural comparison of the enzyme structure with RfbC homologues shows that the key active-site residues are conserved across kingdoms. RmlC-like epimerases belongs to the diverse cupin superfamily
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evolution
Haloferax volcanii WR536 / H53 / ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
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Archaea synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses
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malfunction
rhamnose and N-acetyl-galactosamine are not detected, and fucose is greatly diminished in the rmlC mutant (transposon pLOF/Sp inserted into rmlC (TDP-4-keto-6-deoxy-D-glucose 3,5-epimerase) compared with that in the wild-type strain)
malfunction
disruption of rmbC results in fragmented mycelia that quickly convert into gray pigmented spores
malfunction
the expression of the rhamnose biosynthetic genes by RNAi results in significant reductions in dTDP-rhamnose, but has no effect on the biosynthesis of a closely related sugar, ascarylose, found in the ascaroside pheromones. RNAi against rml-3 does not affect embryonic or larval development
malfunction
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disruption of rmbC results in fragmented mycelia that quickly convert into gray pigmented spores
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metabolism
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dTDP-4-dehydrorhamnose 3,5-epimerase is an enzyme which may be associated with the cellulose synthesis-reducing effect of the mutation in strain K3
metabolism
the enzyme is required for L-rhamnose synthesis
metabolism
the enzyme from the doxorubicin biosynthesis gene cluster is involved in the biosynthesis of dTDP-L-daunosamine, pathway overview. It does not compensate for the other dTDP-4-keto-6-deoxyglucose 3,5-epimerase encoded by gene rmbC. Although dnmU and rmbC encode for similar functional proteins, their native roles in their respective biosynthetic pathways in vivo are specific and independent of one other
metabolism
the enzyme is involved in the biosynthesis of dTDP-L-rhamnose, a precursor of cell wall biosynthesis, pathway overview. It does not compensate for the other dTDP-4-keto-6-deoxyglucose 3,5-epimerase encoded by gene dnmU. Although dnmU and rmbC encode for similar functional proteins, their native roles in their respective biosynthetic pathways in vivo are specific and independent of one other
metabolism
Archaea synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses. The pathwayto synthesize nucleotide-activated rhamnose involves Agl11 as a glucose-1-phosphate thymidylyltransferase, Agl12 as a dTDP-glucose-4,6-dehydratase, Agl13 as a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase, and Agl14 as a dTDP-4-dehydrorhamnose reductase
metabolism
biosynthesis of dTDP-L-rhamnose: RML-1 activates glucose 1-phosphate in the presence of either dTTP or UTP to yield dTDP-glucose or UDP-glucose, respectively. RML-2 is a dTDP-glucose 4,6-dehydratase, converting dTDP-glucose into dTDP-4-keto-6-deoxyglucose. And coincubation of dTDP-4-keto-6-deoxyglucose with RML-3 (3,5-epimerase) and RML-4 (4-keto-reductase) produces dTDP-rhamnose. A co-regulated protein, RML-5, forms a complex with RML-4. Rhamnose biosynthesis may play an important role in hypodermal development or the production of the cuticle or surface coat during molting
metabolism
Q81TP1
the biosynthetic pathway used to form the activated L-rhamnose donor dTDP-L-rhamnose consists of four enzymes, RfbA, RfbB, RfbC and RfbD. RfbC catalyzes the third reaction, a double epimerization producing dTDP-6-deoxy-L-lyxo-4-hexulose (dTDP-4-dehydro-L-rhamnose)
metabolism
the enzyme is involved in the dTDP-rhamnose biosynthetic pathway
metabolism
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the biosynthetic pathway used to form the activated L-rhamnose donor dTDP-L-rhamnose consists of four enzymes, RfbA, RfbB, RfbC and RfbD. RfbC catalyzes the third reaction, a double epimerization producing dTDP-6-deoxy-L-lyxo-4-hexulose (dTDP-4-dehydro-L-rhamnose)
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metabolism
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the enzyme is involved in the biosynthesis of dTDP-L-rhamnose, a precursor of cell wall biosynthesis, pathway overview. It does not compensate for the other dTDP-4-keto-6-deoxyglucose 3,5-epimerase encoded by gene dnmU. Although dnmU and rmbC encode for similar functional proteins, their native roles in their respective biosynthetic pathways in vivo are specific and independent of one other
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metabolism
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the enzyme from the doxorubicin biosynthesis gene cluster is involved in the biosynthesis of dTDP-L-daunosamine, pathway overview. It does not compensate for the other dTDP-4-keto-6-deoxyglucose 3,5-epimerase encoded by gene rmbC. Although dnmU and rmbC encode for similar functional proteins, their native roles in their respective biosynthetic pathways in vivo are specific and independent of one other
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metabolism
Haloferax volcanii WR536 / H53 / ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
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Archaea synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses. The pathwayto synthesize nucleotide-activated rhamnose involves Agl11 as a glucose-1-phosphate thymidylyltransferase, Agl12 as a dTDP-glucose-4,6-dehydratase, Agl13 as a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase, and Agl14 as a dTDP-4-dehydrorhamnose reductase
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physiological function
the rmlC mutant strain colonizes the rabbit mitral valves approximately 3fold less effectively than the wild type strain
physiological function
enzyme Agl13 is a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase
physiological function
Q81TP1
the exosporium layer of Bacillus anthracis spores is rich in L-rhamnose, a common bacterial cell-wall component, which often contributes to the virulence of pathogens by increasing their adherence and immune evasion. The biosynthetic pathway used to form the activated L-rhamnose donor dTDP-L-rhamnose consists of four enzymes, RfbA, RfbB, RfbC and RfbD. The dTDP-4-dehydrorhamnose 3,5-epimerase, RfbC, epimerizes dTDP-4-dehydro-6-deoxy-alpha-D-glucose into dTDP-4-dehydro-beta-L-rhamnose
physiological function
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the exosporium layer of Bacillus anthracis spores is rich in L-rhamnose, a common bacterial cell-wall component, which often contributes to the virulence of pathogens by increasing their adherence and immune evasion. The biosynthetic pathway used to form the activated L-rhamnose donor dTDP-L-rhamnose consists of four enzymes, RfbA, RfbB, RfbC and RfbD. The dTDP-4-dehydrorhamnose 3,5-epimerase, RfbC, epimerizes dTDP-4-dehydro-6-deoxy-alpha-D-glucose into dTDP-4-dehydro-beta-L-rhamnose
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physiological function
Haloferax volcanii WR536 / H53 / ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
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enzyme Agl13 is a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase
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additional information
Q81TP1
two different ligands are bound in the protein structure: diphosphate in the active site of one monomer and dTDP in the other monomer, active site structure, overview
additional information
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two different ligands are bound in the protein structure: diphosphate in the active site of one monomer and dTDP in the other monomer, active site structure, overview
additional information
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two different ligands are bound in the protein structure: diphosphate in the active site of one monomer and dTDP in the other monomer, active site structure, overview
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