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α-Keto Acid Dehydrogenation Complexes
Open accessAbstract
Enzyme systems that catalyze the lipoic acid-mediated oxidative decarboxylation of pyruvate (Reaction 1) have been isolated from pigeon breast muscle (1, 2) and from Escherichiu coli (3) as Pyruvate + CoA-SH + DPNf --) acetyl-S-Co;i multienzyme complexes with molecular weights of approximately 4 and 4.8 million, respectively. Enzyme complexes that catalyze an analogous decomposition of a-ketoglutarate have been isolated from pig heart (4) and from E. coli (3). It has been pre-sumed that as many as four separate enzymes are involved in overall Reaction 1, since the latter reaction apparently occurs in a sequence of four steps (5,6) as shown in Equations 2 to 5, where the brackets indicate enzyme-bound compounds. However,
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Cited by
Structure-function relationships in dihydrolipoamide acyltransferases.
Reed, L. J., & Hackert, M. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38795-2 · Cited by 377
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-citationThe pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
de Kok, A., Hengeveld, A. F., Martin, A., & Westphal, A. H. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00079-x · Cited by 174
Metadata
- Authors
- Koike, M., Reed, L. J., & Carroll, W. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1963-01
- Volume
- 238
- Issue
- 1
- Pages
- 30-39
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1518644765
- Cited by
- 241
- References
- 0
- FWCI
- 3.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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