enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose
an engineered Escherichia coli strain, with functional co-expression of a xylose dehydrogenase (gene xdh) and a xylonolactonase (gene xylC) from Caulobacter crescentus, has a promising perspective for large-scale production of xylonate
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected
gene xylC, functional co-expression of a xylose dehydrogenase (gene xdh) and a xylonolactonase (gene xylC) from Caulobacter crescentus in Escherichia coli strain BL21DELTAxylAB, lacking functional genes xylA and xylB encoding xylose isomerase and xylulose kinase, which compete for D-xyylose with xylose dehydrogenase
considerable interest exists in utilizing the hemicellulose biomass for fine chemical production by converting xylose microbially to xylonic acid, other proposed uses of xylonic acid are in textile bleaching or in electroplating
an engineered Escherichia coli strain, with functional co-expression of a xylose dehydrogenase (gene xdh) and a xylonolactonase (gene xylC) from Caulobacter crescentus, has a promising perspective for large-scale production of xylonate
construction of a route for glycolate production in Escherichia coli by introducing NAD+-dependent xylose dehydrogenase xdh and xylonolactonase xylC from Caulobacter crescentus. The engineered strain produces 28.82 g/L glycolate from xylose with 0.60 g/L/h productivity and 0.38 g/g xylose yield. 27.18 g/L acetate accumulates after fermentation. An ackA knockout results in about 66% decrease in acetate formation. The final engineered strain produces 43.60 g/L glycolate, with 0.91 g/L/h productivity and 0.46 g/g xylose yield
construction of a route for glycolate production in Escherichia coli by introducing NAD+-dependent xylose dehydrogenase xdh and xylonolactonase xylC from Caulobacter crescentus. The engineered strain produces 28.82 g/L glycolate from xylose with 0.60 g/L/h productivity and 0.38 g/g xylose yield. 27.18 g/L acetate accumulates after fermentation. An ackA knockout results in about 66% decrease in acetate formation. The final engineered strain produces 43.60 g/L glycolate, with 0.91 g/L/h productivity and 0.46 g/g xylose yield