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Literature summary for 1.2.1.12 extracted from

  • Martinez, I.; Zhu, J.; Lin, H.; Bennett, G.N.; San, K.Y.
    Replacing Escherichia coli NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with a NADP-dependent enzyme from Clostridium acetobutylicum facilitates NADPH dependent pathways (2008), Metab. Eng., 10, 352-359.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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General Information

General Information Comment Organism
metabolism replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains Escherichia coli