Work

Sugar Synthesis in Leptospira

Year: 1984

Type: article

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.

Source: Microbiology and Immunology

DOI: 10.1111/j.1348-0421.1984.tb00670.x

Authors: Yasutake Yanagihara, Susumu Kobayashi, Ichiji Mifuchi

Institution: University of Shizuoka

Language: English

Topic: Leptospirosis research and findings

Subfield: Parasitology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W1895276707

FWCI: 0.941

Cites: 36

Cited by: 6

Related to: 10