Recombinant l-glutaminase obtained from Geobacillus thermodenitrificans DSM-465: characterization and in silico elucidation of conserved structural domains.

ABSTRACT: Glutaminase (GLS) is an enzyme essential for amino acid metabolism; in particular, it acts as a catalyst in glutaminolysis, a reaction exploited by the malignant cells to meet the nutrient requirements for their accelerated growth and proliferation. Via regulating the initial reaction of the glutaminolysis pathway, glutaminase offers an intriguing target for the development of anticancer drugs. In the present study, we produced a recombinant glutaminase from Geobacillus thermodenitrificans DSM-465 in E. coli. The enzyme was purified to electrophoretic homogeneity, with 40% recovery and 22.36 fold purity. It exhibited a molecular weight of 33 kDa, with an optimum pH and temperature of 9 and 70 °C, respectively. The K _M value of the purified enzyme was

SUBMITTER: Shah L 

PROVIDER: S-EPMC9060542 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature