Abstract
The glutaminase (EC 3.5.1.2) isolated from seedlings of triticale (Triticalesp.) had a pH optimum of about 8, was inhibited with excess substrate (glutamine), and reaction products (glutamate and NH+ 4). A monocharged anion (Cl–) and a multicharged anion (phosphate) were shown to activate the glutaminase. Some features of the glutaminase from triticale were similar to those of animal glutaminase activated by phosphate and were different from features of the enzyme from Escherichia coli.
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Sidel'nikova, L.I., Evstigneeva, Z.G., Solov'eva, N.A. et al. Characterization of Glutaminase from Triticale. Applied Biochemistry and Microbiology 37, 569–573 (2001). https://doi.org/10.1023/A:1012394832053
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DOI: https://doi.org/10.1023/A:1012394832053