Purification and Properties of Succinyl‐CoA:3‐Oxo‐Acid CoA‐Transferase from Rat Brain

Russell, Joseph J.; Patel, Mulchand S.

doi:10.1111/j.1471-4159.1982.tb07924.x

Cited by 14 publications

(11 citation statements)

References 25 publications

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“…Therefore, 3-oxoacid CoA-transferase was purified from rat brain to a specific activity of 150 units/mg of protein. The purified enzyme appeared homogeneous on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, as reported previously (Russell & Patel, 1982). The rabbit antisera quantitatively precipitated 3-oxoacid CoA-transferase from extracts of both glioma and neuroblastoma cells which had been radiolabelled with L-[35S]methionine (AgAbl) ( Fig.…”

Section: Resultssupporting

confidence: 82%

“…One unit of enzyme activity is defined as 1 ymol of acetoacetyl-CoA deacylated/ min at 37°C. Purification of3-oxoacid CoA-transferase and generation of specific antiserum 3-Oxoacid CoA-transferase was purified to homogeneity by a previously published procedure (Russell & Patel, 1982), with one modification. The starting material was an extract of frozen rat brain rather than a crude mitochondrial fraction.…”

Section: Cell Culturementioning

confidence: 99%

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Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells

Haney¹,

Bolinger²,

Raefsky³

et al. 1984

Biochemical Journal

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The specific activity of succinyl-CoA:3-oxo-acid CoA-transferase (3-oxoacid CoA-transferase, EC 2.8.3.5) increases significantly during growth in culture in both mouse neuroblastoma N2a and rat glioma C6 cells. To investigate the mechanism(s) responsible for this, antibody specific for rat brain 3-oxoacid CoA-transferase was raised in rabbits. Immunotitrations of 3-oxoacid CoA-transferase from neuroblastoma and glioma cells on days 3 and 7 of growth after subculture showed that the ratio of 3-oxoacid CoA-transferase activity to immunoprecipitable enzyme protein remained constant, indicating that differences in specific activity of the enzyme at these times in both cell types reflect differences in concentration of enzyme protein. In glioma cells, the relative rate of 3-oxoacid CoA-transferase synthesis was about 0.04-0.05% throughout 9 days in culture. In contrast, the relative rate of synthesis of 3-oxo-acid CoA-transferase in neuroblastoma cells was about 0.07-0.08% on days 3, 5 and 7 after subculture, but fell to 0.052% on day 9. The degradation rates of total cellular protein (t1/2 = 28 h) and 3-oxoacid CoA-transferase (t1/2 = 46-50 h) were similar in both cell lines. The rise in specific activity of the enzyme in both cell lines from days 3 to 7 without a significant increase in the relative rate of synthesis reflects a slow approach to steady-state conditions for the enzyme secondary to its slow degradation. Differences in 3-oxoacid CoA-transferase specific activity between the two cell lines are apparently due to a difference of about 60% in relative rates of enzyme synthesis. The presence of 0.5 mM-acetoacetate in the medium significantly increased the specific activity of 3-oxoacid CoA-transferase in neuroblastoma cells during the early exponential growth phase. This treatment increased the relative rate of synthesis of 3-oxoacid CoA-transferase by 23% (P less than 0.025) in these cells on day 3, suggesting that substrate-mediated induction of enzyme synthesis is a mechanism of regulation of 3-oxoacid CoA-transferase.

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Section: Resultssupporting

confidence: 82%

Section: Cell Culturementioning

confidence: 99%

Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells

Haney¹,

Bolinger²,

Raefsky³

et al. 1984

Biochemical Journal

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“…They have been identified in many prokaryotes (5)(6)(7)(8)(9)(10)(11)(12) and in mammalian tissues (13)(14)(15)(16)(17)(18). Although the CoA-transferases appear to be mechanistically and functionally very similar (5,6,10), their substrate ranges and activities differ.…”

mentioning

confidence: 99%

Cloning and Characterization of Helicobacter pyloriSuccinyl CoA:Acetoacetate CoA-transferase, a Novel Prokaryotic Member of the CoA-transferase Family

Corthésy–Theulaz¹,

Bergonzelli²,

Henry³

et al. 1997

Journal of Biological Chemistry

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“…and mammalian tissues (3,44,48,59). Although the substrate ranges and subunit structures may differ, CoA transferases appear to be mechanistically and functionally very similar (2,24,51,57,62).…”

mentioning

confidence: 99%

Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida

Parales

Harwood

1992

J Bacteriol

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beta-Ketoadipate:succinyl-coenzyme A transferase (beta-ketoadipate:succinyl-CoA transferase) (EC 2.8.3.6) carries out the penultimate step in the conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates in bacteria utilizing the beta-ketoadipate pathway. This report describes the characterization of a DNA fragment from Pseudomonas putida that encodes this enzyme. The fragment complemented mutants defective in the synthesis of the CoA transferase, and two proteins of sizes appropriate to encode the two nonidentical subunits of the enzyme were produced in Escherichia coli when the fragment was placed under the control of a phage T7 promoter. DNA sequence analysis revealed two open reading frames, designated pcaI and pcaJ, that were separated by 8 bp, suggesting that they may comprise an operon. A comparison of the deduced amino acid sequence of the P. putida CoA transferase genes with the sequences of two other bacterial CoA transferases and that of succinyl-CoA:3-ketoacid CoA transferase from pig heart suggests that the homodimeric structure of the mammalian enzyme may have resulted from a gene fusion of the bacterial alpha and beta subunit genes during evolution. Conserved functional groups important to the catalytic activity of CoA transferases were also identified.

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Purification and Properties of Succinyl‐CoA:3‐Oxo‐Acid CoA‐Transferase from Rat Brain

Cited by 14 publications

References 25 publications

Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells

Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells

Cloning and Characterization of Helicobacter pyloriSuccinyl CoA:Acetoacetate CoA-transferase, a Novel Prokaryotic Member of the CoA-transferase Family

Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida

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