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Literature summary for 4.2.1.82 extracted from

  • Meijnen, J.P.; de Winde, J.H.; Ruijssenaars, H.J.
    Establishment of oxidative D-xylose metabolism in Pseudomonas putida S12 (2009), Appl. Environ. Microbiol., 75, 2784-2791.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
xylXABCD, xylXAD, xylXD, xylD or xylX ligated into the vector pJTmcs using the KpnI, XbaI, and XmaJI restriction sites, under the control of the constitutive tac promoter, expressed in Pseudomonas putida S12 Caulobacter vibrioides

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Caulobacter vibrioides

Organism

Organism UniProt Comment Textmining
Caulobacter vibrioides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose
-
 Caulobacter vibrioides 2-dehydro-3-deoxy-D-xylonate + H2O
-
 ?

Synonyms

Synonyms Comment Organism
D-xylonate dehydratase
-
 Caulobacter vibrioides
XYLD
-
 Caulobacter vibrioides

General Information

General Information Comment Organism
metabolism is essential for establishing an oxidative D-xylose catabolic pathway in Pseudomonas putida S12, but coexpression of the putative 2-keto-3-deoxy-D-xylonate dehydratase (XylX) improves the biomass yield by approximately 10%, while the growth rate is not altered. When XylA, catalyzing the next and final step in the pathway, is also coexpressed, both the biomass yield and the maximum growth rate increase. Lower-pathway activities of strains S12xylXD and S12xylD, which rely on endogenous semialdehyde dehydrogenase, are about one-half the activity of the strain that coexpresses the alpha-KGSA dehydrogenase (S12xylXAD) Caulobacter vibrioides