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.
References
40
Referenced
26
10.1042/bj0920010C
10.1042/bj0920010C
/ Biochem. J. by Garland P. B. (1964)10.1016/0926-6593(66)90076-2
10.1016/0006-291X(68)90504-4
10.1073/pnas.62.1.234
10.1073/pnas.64.1.227
10.1016/0014-5793(69)80156-0
10.1021/bi00808a019
10.1021/bi00851a035
10.1016/S0021-9258(18)62650-X
10.1111/j.1432-1033.1975.tb02460.x
10.1016/0003-9861(59)90090-6
10.1021/bi00851a033
{'key': 'e_1_2_3_15_2', 'volume-title': 'Methoden der enzymatischen Analyse', 'author': 'Bergmeyer H. U.', 'year': '1970'}
/ Methoden der enzymatischen Analyse by Bergmeyer H. U. (1970)10.1016/0926-6593(66)90019-1
/ Biochim. Biophys. Acta by Hayakawa T. (1966)10.1016/S0021-9258(18)91827-2
10.1093/oxfordjournals.jbchem.a129828
/ J. Biochem. (Tokyo) by Hirabayaschi T. (1972)10.1016/0003-9861(70)90393-0
10.1016/S0021-9258(18)62711-5
/ J. Biol. Chem. by Poulsen L. L. (1970)10.1021/bi00865a047
10.1111/j.1432-1033.1975.tb02462.x
{'key': 'e_1_2_3_23_2', 'volume-title': 'The Enzymes', 'author': 'Dixon M.', 'year': '1964'}
/ The Enzymes by Dixon M. (1964)10.1016/S0021-9258(18)97380-1
10.1016/0014-5793(72)80257-6
{'key': 'e_1_2_3_26_2', 'first-page': '217', 'volume-title': 'Structure and Function of Enzymes', 'author': 'Veeger C.', 'year': '1971'}
/ Structure and Function of Enzymes by Veeger C. (1971)- Van denBroek H. W. J.(1971)Thesis Agricultural University Wageningen Mededelingen Landbouwhogeschool Wageningen pp.71–78.
- VanMuiswinkel‐Voetberg H.(1972)Thesis Agricultural University Wageningen Mededelingen Landbouwhogeschool Wageningen pp.72–74.
10.1016/0006-3002(62)90762-X
10.1016/0014-5793(72)80630-6
10.1111/j.1432-1033.1972.tb01783.x
10.1111/j.1432-1033.1971.tb19696.x
10.1111/j.1432-1033.1969.tb00559.x
10.1016/0003-9861(72)90504-8
10.1016/0003-9861(71)90194-9
10.1016/0003-9861(72)90152-X
10.1515/bchm2.1969.350.1.329
10.1016/S0021-9258(19)43138-4
10.1111/j.1432-1033.1975.tb09817.x
{'key': 'e_1_2_3_40_2', 'volume-title': 'Proc. 5th Symposium on Flavins and Flavoproteins', 'author': 'Veeger C.'}
/ Proc. 5th Symposium on Flavins and Flavoproteins by Veeger C.10.1016/S0022-2836(65)80285-6
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) |
@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} }