title: Sugar synthesis in Leptospira. I. Presence of glucosephosphate isomerase.
abstract: The presence of glucosephosphate isomerase, one of the key enzymes in carbohydrate metabolism, was confirmed for the first time in the cell-free extract of Leptospira biflexa. The glucosephosphate isomerase of L. biflexa was heat-labile and its optimum pH was about 8.5. The enzyme showed an optimal temperature of about 45 C but was more stable at 30 C. Km value of the enzyme was 5.6 X 10(-3)M. The activity of the enzyme was inhibited by the inhibitor, 6-phosphogluconate. From this study, the presence of a metabolic pathway, the phosphogluconate pathway, other than non-oxidative pentose phosphate pathway presented by Baseman and Cox was suggested.
mesh_terms: D002952:Citric Acid Cycle; D005636:Fructosephosphates / Q000378:metabolism*; D005942:Gluconates / Q000494:pharmacology; D019298:Glucose-6-Phosphate; D005956:Glucose-6-Phosphate Isomerase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005958:Glucosephosphates / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007919:Leptospira / Q000201:enzymology* / Q000378:metabolism; D013696:Temperature
chemical_list: D005636:Fructosephosphates; D005942:Gluconates; D005958:Glucosephosphates; D019298:Glucose-6-Phosphate; C027618:fructose-6-phosphate; D005956:Glucose-6-Phosphate Isomerase; C008884:6-phosphogluconic acid