Summary
In this paper a steady-state kinetic study on the system lactate dehydrogenase-β-thiopyruvate-β-thiolactate is presented and the possible mechanistic and physiological implications are discussed.
At pH 7.4 the equilibrium between β-thiopyruvate and β-thiolactate, in the presence of NADH and lactate dehydrogenase is largerly shifted towards the formation of β-thiolactate as in the case of pyruvate and lactate. This can be relevant in connection with the mixed disulfide between cysteine and β-thiolactate that is observed to be present in the mammalian body fluids.
The catalytic mechanism is of the bi-bi compulsory order type, and rapid equilibrium conditions for the binding of the first substrate (NADH) are shown to apply. A complex inhibition pattern of inhibitions by both substrates, however, prevents simple suggestions about the nature of the dead-end species involved.
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Abbreviations
- TPA:
-
β-thiopyruvic acid
- TLA:
-
β-thiolactic acid
- E:
-
enzyme
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This work is gratefully dedicated to Prof. Alessandro Rossi Fanelli on the occasion of his 75th birthday.
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Pensa, B., Costa, M., Colosimo, A. et al. Reduction of β-thiopyruvic acid by lactate dehydrogenase: a kinetic study. Mol Cell Biochem 44, 107–112 (1982). https://doi.org/10.1007/BF00226894
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DOI: https://doi.org/10.1007/BF00226894