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Literature summary for 1.1.1.119 extracted from

  • Schewe, H.; Kaup, B.A.; Schrader, J.
    Improvement of P450(BM-3) whole-cell biocatalysis by integrating heterologous cofactor regeneration combining glucose facilitator and dehydrogenase in E. coli (2008), Appl. Microbiol. Biotechnol., 78, 55-65.
    View publication on PubMed
Search for more literature for 1.1.1.119

Application

Application Comment Organism
industry Optimizing whole-cell biocatalysts by integrating a recombinant intracellular NADPH regeneration system through co-expression of a glucose facilitator from Zymomonas mobilis for uptake of unphosphorylated glucose and a NADP+-dependent glucose dehydrogenase from Bacillus megaterium that oxidizes glucose to gluconolactone. Priestia megaterium
synthesis Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions Priestia megaterium

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) already heterologously overexpressing P450 BM-3 QM together with glucose facilitator (GLF) from Zymomonas mobilis Priestia megaterium
expression in Escherichia coli, together with a glucose facilitator from Zymomonas mobilis for uptake of unphosphorylated glucose Priestia megaterium

Protein Variants

Protein Variants Comment Organism
additional information Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions Priestia megaterium
additional information introduction of both, GLF and GlcDH, in P450-overexpressing Escherichia coli should enable the cell to carry out a straightforward intracellular cofactor regeneration driven by externally added glucose. For the generation of recombinant Escherichia coli strains carrying two plasmids, these are transformed successively. Firstly, pZY507glf is transformed into Escherichia coli BL21 (DE3). Subsequently, competent cells are prepared from a positive transformant, and then pETDUETbm-3qm glcdh is transformed. Priestia megaterium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + NADP+ Priestia megaterium unphosphorylated glucose as substrate D-glucono-1,5-lactone + NADPH + H+
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 ?

Organism

Organism UniProt Comment Textmining
Priestia megaterium
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-
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Priestia megaterium
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 expression in Escherichia coli BL21 (DE3) already heterologously overexpressing P450 BM-3 QM together with glucose facilitator (GLF) from Zymomonas mobilis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NADP+ unphosphorylated glucose as substrate Priestia megaterium D-glucono-1,5-lactone + NADPH + H+
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 ?

Synonyms

Synonyms Comment Organism
GlcDH 2
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 Priestia megaterium
glucose dehydrogenase
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 Priestia megaterium