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Literature summary for 5.5.1.2 extracted from

  • Eulberg, D.; Lakner, S.; Golovleva, L.A.; Schlömann, M.
    Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity (1998), J. Bacteriol., 180, 1072-1081.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rhodococcus opacus enzyme of the protocatechuate branch of the beta-ketoadipate pathway ?
-
?
additional information Rhodococcus opacus 1CP enzyme of the protocatechuate branch of the beta-ketoadipate pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus
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-
-
Rhodococcus opacus 1CP
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-Carboxy-2,5-dihydro-5-oxofuran-2-acetate i.e. beta-carboxy-cis,cis-muconate Rhodococcus opacus cis-Butadiene-1,2,4-tricarboxylate i.e. gamma-carboxymuconolactone ?
2-Carboxy-2,5-dihydro-5-oxofuran-2-acetate i.e. beta-carboxy-cis,cis-muconate Rhodococcus opacus 1CP cis-Butadiene-1,2,4-tricarboxylate i.e. gamma-carboxymuconolactone ?
additional information enzyme of the protocatechuate branch of the beta-ketoadipate pathway Rhodococcus opacus ?
-
?
additional information enzyme of the protocatechuate branch of the beta-ketoadipate pathway Rhodococcus opacus 1CP ?
-
?