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Literature summary for extracted from

  • Sans, C.; Garcia-Fruitos, E.; Ferraz, R.M.; Gonzalez-Montalban, N.; Rinas, U.; Lopez-Santin, J.; Villaverde, A.; Alvaro, G.
    Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts (2012), Biotechnol. Prog., 28, 421-427.
    View publication on PubMed


Application Comment Organism
synthesis expression of fuculose-1-phosphate aldolase FucA in Escherichia coli as active inclusion bodies in batch cultures and modulation of the activity of insoluble FucA by a proper selection of producing strain, culture media, and process conditions. In an optimized defined medium, FucA inclusion bodies are more active (in terms of specific activity) than the soluble protein version obtained in the same process with a conventional defined medium. Either directly or immobilized into LentikatVR beads, FucA gives product yields ranging from 65 to 76% in an aldolic reaction between DHAP and (S)-Cbz-alaninal Escherichia coli


Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate + (S)-Cbz-alaninal
Escherichia coli ?


Synonyms Comment Organism
Escherichia coli