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S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
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S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
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additional information
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the RLP can catalyze an overall 1,3-proton transfer reaction via two successive 1,2-proton transfer reactions initiated by abstraction of the 3-proton of the substrate, and the RLP catalyzes a second 1,2-proton transfer reaction initiated by abstraction of the 4-proton from the 3-oxo intermediate to generate a second 3,4-enediolate anion. A bidentate coordination with Mg2+ to stabilize both the 2,3- and 3,4-enediolate intermediates is expected to require movement of the Mg2+ and/or the substrate on the reaction coordinate, although the same base could catalyze abstraction of a proton from carbon-3 of the substrate and carbon-4 of the presumed 3-keto intermediate. Continuous monitoring of the reaction by 1H NMR does not reveal transient accumulation of the 3-keto intermediate, suggesting that it remains enzyme-bound during the course of the reaction
evolution
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
evolution
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the enzyme is a member of the RuBisCO superfamily, RuBisCO catalyzes carboxylation and oxygenation, while the enzyme from Rhodospirillum rubrum catalyzes isomerizations, overview. Rhodospirillum rubrum encodes an RLP that is a member of an uncharacterized family of RLPs which contain a KDDH motif instead of the signature KDDE motif. Like the tautomerases, the sequences contain hydrophobic residues (Pro and Ile/Val) for the formation of a hydrophobic binding pocket for the distal portion of the substrate. The enzyme is able to utilize 5'-methythioadenosine (MTA) as a sulfur source
evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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malfunction
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disruption of the gene encoding the RLP abolishes the ability of Rhodospirillum rubrum to utilize 5'-methylthioadenosine (MTA) as a sole sulfur source, implicating a distinct pathway for sulfur salvage
malfunction
disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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metabolism
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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physiological function
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some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP enzyme from Rhodospirillum rubrum catalyzes an isomerization reaction (overall 1,3-proton transfer reaction, likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate. Role of this RLP in a sulfur salvage pathway
physiological function
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
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the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.