EC Number   |
General Information |
Reference |
|---|
   3.1.1.31 | malfunction |
pgl deletion mutant has decreased growth in glucose-limiting minimal medium but grows normally when excess glucose is added. The Pgl deletion mutant has increased expression of several beta-glucosidases, consistent with inhibition of beta-glucosidases by 6-phosphogluconolactone, it accumulates and secretes a glucose-derived metabolite. Pgl deletion enhances activation of host IFN-beta expression independently of mdrM. At 48 h after infection of mice with 1 50% lethal dose, the pgl deletion mutant exhibits a 15- to 30fold growth defect in the liver and spleen. Pgl deletion mutant is more sensitive to oxidative stress, i.e., to diamide and hydrogen peroxide but not to the antibiotic control |
708705 |
| 3.1.1.31 | malfunction |
pgl3 mutation knocks out most of the 6PGL activity. Knockdown of PGL3 leads to a dramatic decrease in plant size, a significant increase in total glucose-6-phosphate dehydrogenase activity and a marked decrease in cellular redox potential. A wild-type PGL3-GFP transgene complements all phenotypes caused by the pgl3 mutation. Plastidic localization and enzymatic activity are required for PGL3 to complement the pgl3 mutant phenotypes. Pgl3 mutation exhibits constitutive pathogenesis-related gene expression and enhanced resistance to Pseudomonas syringae pv. maculicola ES4326 and Hyaloperonospora arabidopsidis Noco2. The pgl3 mutation activates NPR1- and SID2/EDS16/ICS1-dependent defense signaling |
710266 |
| 3.1.1.31 | metabolism |
in Plasmodium falciparum, glucose-6-phosphate dehydrogenase is combined with the second enzyme of the pentose phosphate pathway to create a unique bifunctional enzyme named GluPho, glucose-6-phosphate dehydrogenase/6-phosphogluconolactonase. The G6PD activity is not largely influenced by the 6PGL part |
714104 |
| 3.1.1.31 | metabolism |
the enzyme is one of the six enzymes of the pentose phosphate pathway of Trypanosoma brucei and hydrolyzes D-6-phosphogluconolactone to 6-phosphogluconic acid |
730906 |
| 3.1.1.31 | more |
analysis of effects of ligand binding on the internal dynamics of the enzyme by molecular dynamics simulations and nuclear magnetic resonance, alterations of conformational exchange, overview. Residues R77 and R200, located near the active site, interact directly with the phosphate group of 6-phospho-D-gluconate. Residue H165 is actively involved in catalysis |
730906 |
| 3.1.1.31 | physiological function |
a pglA deletion mutant is impaired in both pathogenesis and gut persistence in Manduca sexta and produces enhanced biofilms compared with the wild type in an in vitro polystyrene plate assay |
750732 |
| 3.1.1.31 | physiological function |
PGL1 is dispensable for plant growth and development |
710266 |
| 3.1.1.31 | physiological function |
PGL2 is dispensable for plant growth and development |
710266 |
| 3.1.1.31 | physiological function |
PGL3 is the major contributor to total 6PGL activity. PGL3 is essential for plant growth and development. Plastidic localization and 6PGL activity of the PGL3 protein are essential for complementing all pgl3 phenotypes, indicating that the oxidative section of the plastidic pentose phosphate pathway is required for plant normal growth and development. PGL3 may function downstream of salicylic acid |
710266 |
| 3.1.1.31 | physiological function |
PGL5 is dispensable for plant growth and development |
710266 |
