Sugar synthesis in Leptospira. I. Presence of glucosephosphate isomerase.
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.
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
D005636:Fructosephosphates; D005942:Gluconates; D005958:Glucosephosphates; D019298:Glucose-6-Phosphate; C027618:fructose-6-phosphate; D005956:Glucose-6-Phosphate Isomerase; C008884:6-phosphogluconic acid