A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

Peter Butterworth; Chun-Chien Tsai; Michael H. Eley; T.E. Roche; Lester J. Reed

doi:10.1016/s0021-9258(19)41783-3

March 1, 1975Journal of Biological ChemistryOpen Access

A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

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Key Points

To elucidate the kinetic mechanism and catalytic site structure of dihydrolipoyl transacetylase isolated from bovine kidney.
Monitored the transfer of labeled acetyl groups using a model reaction between [1-14C]acetyl-CoA and dihydrolipoamide.
Performed initial velocity, product inhibition, and dead-end inhibition assays in the presence and absence of pyruvate dehydrogenase, dihydrolipoyl dehydrogenase, their substrates/products, and covalently bound lipoyl groups.
The transacetylase model reaction was not affected by the presence of pyruvate dehydrogenase, dihydrolipoyl dehydrogenase, their associated substrates or products, or removal of the lipoyl moiety.
Inhibition and velocity patterns showed the reaction proceeds through a rapid equilibrium Random Bi Bi mechanism with two adjacent catalytic sites: one binding CoA/acetyl-CoA and the other binding dihydrolipoamide/S-acetyldihydrolipoamide.

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Implication

In vitro kinetic study reveals that dihydrolipoyl transacetylase operates via a Random Bi Bi mechanism in bovine kidney, indicating the presence of two adjacent catalytic binding sites.

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Butterworth et al. (1975) studied this question.

synapsesocial.com/papers/6a7011375d37378ac1dd1e7a https://doi.org/10.1016/s0021-9258(19)41783-3

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A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

Key Points

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Implication

Discussion

Cite This Study

A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

Key Points

No abstract yet

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Implication

Discussion

Cite This Study

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