Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Corynebacterium glutamicum and UniProt Accession Q01651
for references in articles please use BRENDA:EC1.2.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
The taxonomic range for the selected organisms is: Corynebacterium glutamicum The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
the wild-type enzyme shows no activity with NADP+. The carboxylate group of Asp35 forms a network of hydrogen bonds with the 2' and 3-hydroxylgroups of the adenosine ribose ring of NAD+. This seems to be a critical factor to discriminate against the 2'-phosphate group of NADP+, because of electrostatic repulsion between the carboxylate group and phosphate group. Mutation of residues D35, L36, T37, and P192 alters the enzyme's cofactor specificity. Molecular docking and modelling
the wild-type enzyme shows no activity with NADP+. The carboxylate group of Asp35 forms a network of hydrogen bonds with the 2' and 3-hydroxylgroups of the adenosine ribose ring of NAD+. This seems to be a critical factor to discriminate against the 2'-phosphate group of NADP+, because of electrostatic repulsion between the carboxylate group and phosphate group. Mutation of residues D35, L36, T37, and P192 alters the enzyme's cofactor specificity. Molecular docking and modelling
when endogenous phosphorylating NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Corynebacterium glutamicum is replaced by nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GapN) from Clostridium acetobutylicum, this NADPH-generating glycolytic pathway does not allow for the growth of Corynebacterium glutamicum with glucose as the sole carbon source. Heterologous expression of udhA encoding soluble transhydrogenase from Escherichia coli partly restores growth
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
site-directed mutagenesis, the mutant shows high catalytic efficiency with NADP+ while the catalytic efficiency with NAD+ also increases. The replacement of Pro192 to Ser benefits the binding affinity of both NAD+ and NADP+
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
generation of a de novo NADPH generation pathway by altering the coenzyme specificity of native NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) to NADP, to produce additional NADPH in the glycolytic pathway. Increasing the catalytic efficiency of GAPDH towards NADP enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (60%) is achieved with the mutant showing similar preference towards both NAD and NADP. There is no significant change of flux towards the pentose phosphate pathway and the increased lysine yield is mainly attributed to the NADPH generated by the mutated GAPDH
engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
Metabolic engineering of an ATP-neutral Embden-Meyerhof-Parnas pathway in Corynebacterium glutamicum: growth restoration by an adaptive point mutation in NADH dehydrogenase
A de novo NADPH generation pathway for improving lysine production of Corynebacterium glutamicum by rational design of the coenzyme specificity of glyceraldehyde 3-phosphate dehydrogenase
A de novo NADPH generation pathway for improving lysine production of Corynebacterium glutamicum by rational design of the coenzyme specificity of glyceraldehyde 3-phosphate dehydrogenase