Engineering of Escherichia coli Glyceraldehyde-3-Phosphate Dehydrogenase with Dual NAD⁺/NADP⁺ Cofactor Specificity for Improving Amino Acid Production.

ABSTRACT: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the central metabolism of microbial cells. GAPDHs differ in cofactor specificity and use NAD⁺, NADP⁺, or both cofactors, reducing them to NADH and NADPH, respectively. Sufficient NADPH supply is one of the critical factors required for synthesis of the amino acids l-lysine, l-threonine, and l-proline in industrially important Escherichia coli-based producer strains. E. coli cells have NAD⁺-dependent glycolytic GAPDH. One reasonable approach to increase NADPH formation in cells is to change the specificity of the GAPDH from NAD⁺ to NADP⁺. In this study, we modified the cofactor specificity of E. coli GAPDH by amino acid substitutions at positions 34

SUBMITTER: Slivinskaya EA 

PROVIDER: S-EPMC9145139 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature