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Literature summary for 1.1.1.2 extracted from

  • Wolberg, M.; Filho, M.V.; Bode, S.; Geilenkirchen, P.; Feldmann, R.; Liese, A.; Hummel, W.; Mueller, M.
    Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale (2008), Bioprocess Biosyst. Eng., 31, 183-191.
    View publication on PubMed

Application

Application Comment Organism
synthesis the NADP(H)-dependent enzyme is useful in the selective chemoenzymatic synthesis of the tert-butyl (S)-6-chloro-5-hydroxy-3-ketohexanoate, a highly regio- and enantioselective reduction of a beta,delta-diketohexanoate ester, scale up of the continous fed-batch method, overview Levilactobacillus brevis

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the chemoenzymatic synthesis of the tert-butyl (S)-6-chloro-5-hydroxy-3-ketohexanoate, a highly regio- and enantioselective reduction of a beta,delta-diketohexanoate ester, is catalyzed by the enzyme. The chlorinated diketo ester is converted to the general statin precursor acetonide via the hydroxy keto ester and hydroxyhexanoate, the reaction is reversible, overview Levilactobacillus brevis ?
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Synonyms

Synonyms Comment Organism
LBADH
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Levilactobacillus brevis
NADP(H)-dependent alcohol dehydrogenase
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Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
NADP+ dependent on Levilactobacillus brevis