has a structural role rather than a catalytic one, lies at the center of a tetrahedron. The side chains of H56 and H97 are at a distance of 2.0 A from the metal ion, while the oxygen atom of the carboxylic side chain of D98 coordinates the zinc ion in a monodentate manner. Water molecule at 2.7 A from the metal ion
detailed kinetic analysis of the bifunctional glucose-6-phosphate dehydrogenase/6-phosphogluconolactonase indicates that PfGluPho functions on the basis of a rapid equilibrium random Bi Bi mechanism, where the binding of the second substrate depends on the first substrate
PGL3 contains an N-terminal extension and a C-terminal peroxisome-targeting motif PTS1, subcellular localization of enzyme stages, overview. Besides redox-related and metabolic signals that influence dual-targeting of enzyme PGL3 in leaves, developmental and/or physiological state(s) play another role for subcellular enzyme localization in different plant parts, the metabolic state affects PGL3 targeting by absence/reduced stability of thioredoxin Trxm2
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
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
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
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
PGL1 is dispensable for plant growth and development; PGL2 is dispensable for plant growth and development; 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; PGL5 is dispensable for plant growth and development
the enzyme plays a key role during infection, by providing the important reductive agent NADPH, and forms ribose 5-phosphate, a major nucleic acid precursor, as well as several metabolic intermediates, such as fructose 6-phosphate and glyceraldehyde 3-phosphate
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by the hanging-drop method, 6PGL in complex with two ligands, 6-phosphogluconic acid and citrate, at 2.2 A and 2.0 A resolution, respectively. Structures of the two complexes and of the apo form are almost identical. Both complexes belong to space group P21 and have two molecules in the asymmetric unit, related by a pure translation. PGL in complex with 6-phosphogluconic acid has unit cell parameters of a = 49.66, b = 87, c= 64.91 A and beta = 96.43. PGL in complex with citrate has unit cell parameters of a = 49.46, b = 87.21, c= 64.79 A and beta = 96.53
gene PGL3, presence of the C-terminal SKL motif interfered with chloroplast import of a PGL3_N-full-CFP fusion and with that of a PGL3_long medial-CFP fusion (with free N- and C-terminal ends) exclusively labeling peroxisomes, co-expression of thioredoxin Trxm2 with C-terminally truncated enzyme PGL3_N-short and _N-long versions accumulate in the cytosol of tobacco protoplasts and co-localization with Trxm2 in the cytosol and in the chloroplast stroma, recombinant expression of N-terminally CFP-tagged, green-fluorescent enzyme in Nicotiana benthamiana leaves
PCR product cloned into the corresponding sites of the vector pGEX-4T-1 and then introduced into Escherichia coli. Constructs (35S:DELTANTpgl3-GFP and 35S:pgl3 DELTASKL-GFP) together with the 35S:PGL3-GFP construct transformed into the pgl3 background. Escherichia coli cells expressing GST-PGL3 and GST-pgl3 mutants
Xiong, Y.; DeFraia, C.; Williams, D.; Zhang, X.; Mou, Z.
Characterization of Arabidopsis 6-phosphogluconolactonase T-DNA insertion mutants reveals an essential role for the oxidative section of the plastidic pentose phosphate pathway in plant growth and development