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Literature summary for 1.8.1.5 extracted from

  • Pandey, A.S.; Mulder, D.W.; Ensign, S.A.; Peters, J.W.
    Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2011), FEBS Lett., 585, 459-464.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with acetoacetate and 2-mercaptoethanesulfonate. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group Xanthobacter autotrophicus

Organism

Organism UniProt Comment Textmining
Xanthobacter autotrophicus Q56839
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