The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart
Abstract
The highly purfied pyruvate dehydrogenase complex (EC 1.2.4.1) and uncomplexed pyruvate dehydrogenase from bovine kidney and heart mitochondria were phosphorylated and inactivated with pyruvate dehydrogenase kinase and [gamma-32P]ATP. Tryptic digestion of the phosphorylated pyruvate dehydrogenase yielded three phosphopeptides, a mono- (site 1) and a di- (sites 1 and 2) phosphorylated tetradecapeptide and a monophosphorylated nonapeptide (site 3). The amino acid sequences of the three phosphopeptides were established to be Tyr-His-Gly-His-Ser(P)-Met-Ser-Asn-Pro-Gly-Val-Ser-Tyr-Arg, Tyr-His-Gly-His-Ser(P)-Met-Ser-Asn-Pro-Gly-Val-Ser(P)-Tyr-Arg, and Tyr-Gly-Met-Gly-Thr-Ser(P)-Val-Glu-Arg. Phosphorylation proceeded markedly faster at site 1 than at sites 2 and 3, and phosphorylation at site 1 correlated closely with inactivation of pyruvate dehydrogenase. Complete inactivation of pyruvate dehydrogenase was associated with incorporation at site 1 of 1.0--1.6 mol of phosphoryl groups per mol of enzyme. Since pyruvate dehydrogenase is a tetramer (alpha2beta2) and since phosphorylation occurs only on the alpha subunit, the possibility of half-site reactivity is considered.
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Cites
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Self-citationLinn, T. C., Pettit, F. H., Hucho, F., & Reed, L. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.64.1.227 · Cited by 352
Self-citationRegulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios
Pettit, F. H., Pelley, J. W., & Reed, L. J. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80185-9 · Cited by 314
Self-citationAnomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations
Piszkiewicz, D., Landon, M., & Smith, E. L. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90918-6 · Cited by 291
α-Keto acid dehydrogenase complexes
Linn, T. C., Pelley, J. W., Pettit, F. H., Hucho, F., Randall, D. D., & Reed, L. J. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90151-8 · Cited by 284
Self-citationα-Keto acid dehydrogenase complexes
Barrera, C. R., Namihira, G., Hamilton, L., Munk, P., Eley, M. H., Linn, T. C., & Reed, L. J. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90152-x · Cited by 278
Self-citationα-Keto acid dehydrogenase complexes
Hucho, F., Randall, D. D., Roche, T. E., Burgett, M. W., Pelley, J. W., & Reed, L. J. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90504-8 · Cited by 248
Self-citationSubstrate specificity of the cyclic AMP-dependent protein kinase.
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[4] High-voltage paper electrophoresis
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The Role of Negative Cooperativity and Half-of-the-Sites Reactivity in Enzyme Regulation
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Cited by
The role of protein phosphorylation in neural and hormonal control of cellular activity
Cohen, P. (1982) · Nature · doi:10.1038/296613a0 · Cited by 1,123
Sugden, M. C., & Holness, M. J. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00526.2002 · Cited by 428
The 2-oxo acid dehydrogenase complexes: recent advances
Yeaman, S. J. (1989) · Biochemical Journal · doi:10.1042/bj2570625 · Cited by 330
Self-citationQuinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310
Regulation of pyruvate dehydrogenase complex activity in plant cells
Tovar‐Méndez, A., Miernyk, J. A., & Randall, D. D. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03469.x · Cited by 307
Metadata
- Authors
- Yeaman, S. J., Hutcheson, E. T., Roche, T. E., Pettit, F. H., Brown, J. R., Reed, L. J., Watson, D. C., & Dixon, G. H.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1978-06-13
- Volume
- 17
- Issue
- 12
- Pages
- 2364-2370
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2011646732
- Cited by
- 291
- References
- 15
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- Yeaman, S. J., Hutcheson, E. T., Roche, T. E., Pettit, F. H., Brown, J. R., Reed, L. J., Watson, D. C., & Dixon, G. H. (1978). Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart. Biochemistry. https://doi.org/10.1021/bi00605a017
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