Crossref journal-article
Wiley
European Journal of Biochemistry (311)
Abstract

The presence of activators (AMP and sulphate) or inhibitors (acetyl‐CoA) has no influence on the Hill coefficient of the S‐shaped [pyruvate]–velocity curve of either the pyruvate‐NAD+ overall reaction (h= 2.5) or that of the pyruvate‐K3Fe(CN)6 activity of the first enzyme (h= 1.3). pH studies indicated that the Hill coefficient is dependent on subunit ionization within the pyruvate‐containing complex and not on those in the free complex.It is concluded that pyruvate conversion rather than pyruvate binding is responsible for the allosteric pattern. The activity is, due to absence of a protein kinase, mainly regulated at the acetyl‐CoA/CoA, and NADH/NAD+ levels and by the value of the energy charge.

Bibliography

BRESTERS, T. W., DE KOK, A., & VEEGER, C. (1975). The Pyruvate‐Dehydrogenase Complex from Azotobacter vinelandii. European Journal of Biochemistry, 59(2), 347–353. Portico.

Authors 3
  1. Tjarda W. BRESTERS (first)
  2. Arie DE KOK (additional)
  3. Cees VEEGER (additional)
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Dates
Type When
Created 20 years, 6 months ago (March 3, 2005, 11:16 a.m.)
Deposited 1 year, 10 months ago (Oct. 10, 2023, 9:58 p.m.)
Indexed 1 year, 9 months ago (Nov. 23, 2023, 1:22 p.m.)
Issued 49 years, 10 months ago (Nov. 1, 1975)
Published 49 years, 10 months ago (Nov. 1, 1975)
Published Online 17 years, 2 months ago (June 28, 2008)
Published Print 49 years, 10 months ago (Nov. 1, 1975)
Funders 0

None

@article{BRESTERS_1975, title={The Pyruvate‐Dehydrogenase Complex from Azotobacter vinelandii: 2. Regulation of the Activity}, volume={59}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1975.tb02461.x}, DOI={10.1111/j.1432-1033.1975.tb02461.x}, number={2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={BRESTERS, Tjarda W. and DE KOK, Arie and VEEGER, Cees}, year={1975}, month=nov, pages={347–353} }