Thymidine kinase enzyme variants in <i>Physarum polycephalum</i>; change of pattern during the synchronous mitotic cycle

Gröbner, Peter; Sachsenmaier, W.

doi:10.1016/0014-5793(76)80926-x

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Pyrimidines1

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1986

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Cited by 21 publications

(1 citation statement)

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“…In Physarum polycephalum, the temporal expression of a single thymidine kinase which undergoes post-translational modifications into multiple enzyme variants (GROBNER and SACHSENMAIER 1976), and their modulations through enzyme degradation depending upon temperature (WRIGHT and TOLLON 1979) suggest a more complicated relationship of this enzyme with DNA synthesis. Thus, thymidine incorporation as the measure of DNA synthesis should be carefully verified.…”

Section: Pyrimidinesmentioning

confidence: 99%

Metabolism of Pyrimidines and Purines

Wasternack¹

1982

Nucleic Acids and Proteins in Plants II

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Section: Pyrimidinesmentioning

confidence: 99%

Metabolism of Pyrimidines and Purines

Wasternack¹

1982

Nucleic Acids and Proteins in Plants II

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The PhysarumPhysarum Cell Cycle

Laffler

Tyson

1986

The Molecular Biology of Physarum Polycephalum

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Differences in the kinetic properties of thymidine kinase isoenzymes in unstimulated and phytohemagglutinin-stimulated human lymphocytes

Munch‐Petersen

1984

Mol Cell Biochem

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The two thymidine kinases, TK 1 and TK 2, found in phytohemagglutinin-stimulated human lymphocytes and the thymidine kinase, TK 2N, found in unstimulated human lymphocytes were purified and characterized. All three kinases had molecular weights between 70 000 and 75 000 which increased to 170 000-200 000 in the presence of 2 mM ATP. Studies on the kinetic properties of the enzymes with thymidine and ATP as the substrates and dTTP as the inhibitor showed clear differences between TK 1 and TK 2, but a close similarity between TK 2 and TK 2N. With thymidine as the variable substrate, TK 1 showed Michaelis-Menten kinetics, whereas TK 2 and TK 2N showed characteristic biphasic kinetics. With ATP as the variable substrate, all three enzymes showed positive cooperative kinetics, but TK 2 and TK 2N lost the cooperativity in the presence of dTTP. The results from inhibition studies showed, that dTTP was a cooperative inhibitor of TK 1 but a non-cooperative inhibitor of TK 2 and TK 2N.

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Thymidine kinase enzyme variants in Physarum polycephalum; change of pattern during the synchronous mitotic cycle

Cited by 21 publications

References 13 publications

Metabolism of Pyrimidines and Purines

Metabolism of Pyrimidines and Purines

The PhysarumPhysarum Cell Cycle

Differences in the kinetic properties of thymidine kinase isoenzymes in unstimulated and phytohemagglutinin-stimulated human lymphocytes

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