l-Threonine dehydratase (E.C. 220.127.116.11) activity in the cell-free extracts of the trophozoites of Hartmannella culbertsoni has been purified 20-fold.
The enzyme requires pyridoxal-5-phosphate for its activity and is not cold-labile. Kinetic studies have shown that there is homotropic cooperative interaction between the substrate molecules. The enzyme is susceptible to end-product regulation, l-isoleucine being a feed back inhibitor and l-valine can partially reactivate the l-isoleucine inhibited enzyme. Some nucleotides stimulate the activity of the enzyme indicating allosteric nature of the enzyme.
Certain amoebicidal drugs and antibiotics have marked inhibitory effect on the enzyme.
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Communication no. 1538 from the Central Drug Research Institute, Lucknow, India.
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Raizada, M.K., Mohan Rao, V.K. l-Threonine dehydratase activity of axenically grown Hartmannella culbertsoni . Archiv. Mikrobiol. 84, 119–128 (1972). https://doi.org/10.1007/BF00412432
- Kinetic Study
- Substrate Molecule
- Cooperative Interaction