The enzyme 6-phosphogluconolactonase (EC 3.1.1.31) is present at high levels in bass liver. The enzyme has been purified 1253-fold with an overall yield of 78% in a procedure involving dye-ligand and gel filtration chromatographies. The purified enzyme which is homogenous by all the usual criteria has a molecular weight of about 30,000. It exhibits a considerably high catalytic efficiency with Kcat/Km of 8.5 x 10(7) M-1.s-1 at 22 degrees C. Its activity illustrates the importance of glucose oxidation via the pentose phosphate pathway relative to glycolysis in this organism.
Download full-text PDF |
Source |
---|
Int J Mol Sci
August 2018
Laboratorio de Bioquímica Genética, Instituto Nacional de Pediatría, Secretaría de Salud, Ciudad de México 04530, Mexico.
Glucose-6-phosphate dehydrogenase (G6PD) is the first enzyme in the pentose phosphate pathway and is highly relevant in the metabolism of Previous reports suggested that the G6PD gene is fused with the 6-phosphogluconolactonase (6PGL) gene (). Therefore, in this work, we decided to characterize the fused G6PD-6PGL protein in First, the gene of fused with the gene (::) was isolated from trophozoites of and the corresponding G6PD::6PGL protein was overexpressed and purified in . Then, we characterized the native oligomeric state of the G6PD::6PGL protein in solution and we found a catalytic dimer with an optimum pH of 8.
View Article and Find Full Text PDFMetab Eng Commun
June 2018
Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Australia.
Production of propionic acid by fermentation of propionibacteria has gained increasing attention in the past few years. However, biomanufacturing of propionic acid cannot compete with the current oxo-petrochemical synthesis process due to its well-established infrastructure, low oil prices and the high downstream purification costs of microbial production. Strain improvement to increase propionic acid yield is the best alternative to reduce downstream purification costs.
View Article and Find Full Text PDFMetab Eng
January 2013
Helmholtz Centre for Infection Research, Systems and Synthetic Biology, Braunschweig D-38124, Germany.
Here, we present systems metabolic engineering driven by in-silico modeling to tailor Pseudomonas putida for synthesis of medium chain length PHAs on glucose. Using physiological properties of the parent wild type as constraints, elementary flux mode analysis of a large-scale model of the metabolism of P. putida was used to predict genetic targets for strain engineering.
View Article and Find Full Text PDFBiochem J
June 2011
Interdisciplinary Research Center, Justus Liebig University, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany.
The survival of malaria parasites in human RBCs (red blood cells) depends on the pentose phosphate pathway, both in Plasmodium falciparum and its human host. G6PD (glucose-6-phosphate dehydrogenase) deficiency, the most common human enzyme deficiency, leads to a lack of NADPH in erythrocytes, and protects from malaria. In P.
View Article and Find Full Text PDFArch Biochem Biophys
March 2009
Cardiovascular and Metabolic Diseases, Wyeth Research, Cambridge, MA 02140, USA.
Tissue specific amplification of glucocorticoid action through NADPH-dependent reduction of inactive glucocorticoid precursors by 11beta-hydroxysteroid dehydrogenase (11beta-HSD1) contributes to the development of visceral obesity, insulin resistance and Type 2 Diabetes. Hexose-6-phosphate dehydrogenase (H6PDH) is believed to supply NADPH for the reductase activity of 11beta-HSD1 in the lumen of the endoplasmic reticulum (ER), where the two enzymes are co-localized. We report here expression and purification of full-length and truncated N-terminal domain (NTD) of H6PDH in a mammalian expression system.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!