EC Number   |
General Information |
Reference |
|---|
    1.2.1.59 | malfunction |
the enzyme GapDH interacts with the intrinsically disordered protein CP12, when oxidized but not when reduced, in chloroplasts forming a stable complex. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. The ADK3-GAPDH bienzyme complex is unable to recruit phosphoribulokinase (PRK), in contrast with the ternary complex formed between GAPDH-CP12 and PRK. The interaction between ADK3 and GAPDH might be a mechanism to regulate the crucial ATP: NADPH ratio within chloroplasts to optimize the Calvin-Benson cycle during rapid fluctuation in environmental resources |
763014 |
| 1.2.1.59 | more |
ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH |
763014 |
| 1.2.1.59 | more |
comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance |
-, 762842 |
| 1.2.1.59 | physiological function |
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 NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate |
-, 743222 |
| 1.2.1.59 | physiological function |
in Chlamydomonas reinhardtii, the chloroplast GAPDH is a homotetrameric A4-isoform that lacks regulatory cysteine residues found in the B subunit of the heterotetrameric A2B2-GAPDH isoform. Whereas A2B2-GAPDHs from higher plants are autonomously regulated, CP12 is required to confer redox regulation to the algal A4-GAPDH. In contrast, the CP12-like tail bearing two cysteine residues present on ADK3 is not involved in its redoxregulation |
763014 |
| 1.2.1.59 | physiological function |
phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a ubiquitous cellular enzyme that has a defined role in glycolysis and other pathways where it catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. The enzyme complexes with ADP and might be moonlighting |
763374 |
| 1.2.1.59 | physiological function |
the enzyme plays a key role in glycolysis. GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate |
-, 741524 |
