Literature summary for 1.2.1.9 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.

Search for more literature for 1.2.1.9

Protein Variants

Protein Variants	Comment	Organism
additional information	replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.12 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	Clostridium acetobutylicum

Organism

Organism	UniProt	Comment	Textmining
Clostridium acetobutylicum	-	-	-

General Information

General Information	Comment	Organism
metabolism	replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.12 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	Clostridium acetobutylicum

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)