(en) William T. Wolodko, Cyril M. Kay et William A. Bridger, « Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli », Biochemistry, vol. 25, no 19, , p. 5420-5425 (PMID3535876, DOI10.1021/bi00367a012, lire en ligne)
(en) Michael A. Joyce, Marie E. Fraser, Michael N. G. James, William A. Bridger et William T. Wolodko, « ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography », Biochemistry, vol. 39, no 1, , p. 17-25 (PMID10625475, DOI10.1021/bi991696f, lire en ligne)
(en) Marie E. Fraser, Michael A. Joyce, David G. Ryan et William T. Wolodko, « Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase », Biochemistry, vol. 41, no 2, , p. 537-546 (PMID11781092, DOI10.1021/bi011518y, lire en ligne)
asm.org
jb.asm.org
(en) S. J. Park, G. Chao et R. P. Gunsalus, « Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter », Journal of Bacteriology, vol. 179, no 13, , p. 4138-4142 (PMID9209026, PMCID179232, lire en ligne)
doi.org
dx.doi.org
(en) Marie E. Fraser, Koto Hayakawa, Millicent S. Hume, David G. Ryan et Edward R. Brownie, « Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase », Journal of Biological Chemistry, vol. 281, no 16, , p. 11058-11065 (PMID16481318, DOI10.1074/jbc.M511785200, lire en ligne)
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger3 et William T. Wolodko, « A detailed structural description of Escherichia coli succinyl-CoA synthetase », Journal of Molecular Biology, vol. 285, no 4, , p. 1633-1653 (PMID9917402, DOI10.1006/jmbi.1998.2324, lire en ligne)
(en) Jonathan S. Nishimura, « Succinyl-CoA Synthetase Structure-Function Relationships and Other Considerations », Advances in Enzymology and Related Areas of Molecular Biology, vol. 58, , p. 141-172 (PMID3521216, DOI10.1002/9780470123041.ch4, lire en ligne)
(en) William T. Wolodko, Cyril M. Kay et William A. Bridger, « Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli », Biochemistry, vol. 25, no 19, , p. 5420-5425 (PMID3535876, DOI10.1021/bi00367a012, lire en ligne)
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger et William T. Wolodko, « A detailed structural description of Escherichia coli succinly-CoA synthetase », Journal of Molecular Biology, vol. 288, no 3, , p. 501 (PMID10329157, DOI10.1006/jmbi.1999.2773, lire en ligne)
(en) Michael A. Joyce, Marie E. Fraser, Michael N. G. James, William A. Bridger et William T. Wolodko, « ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography », Biochemistry, vol. 39, no 1, , p. 17-25 (PMID10625475, DOI10.1021/bi991696f, lire en ligne)
(en) Isabel Hunger-Glaser, Reto Brun, Markus Linder et Thomas Seebeck, « Inhibition of succinyl CoA synthetase histidine-phosphorylation in Trypanosoma brucei by an inhibitor of bacterial two-component systems », Molecular and Biochemical Parasitology, vol. 100, no 1, , p. 53-59 (PMID10376993, DOI10.1016/S0166-6851(99)00032-8, lire en ligne)
(en) Marie E. Fraser, Michael A. Joyce, David G. Ryan et William T. Wolodko, « Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase », Biochemistry, vol. 41, no 2, , p. 537-546 (PMID11781092, DOI10.1021/bi011518y, lire en ligne)
(en) James D. Johnson, Wallace W. Muhonen et David O. Lambeth, « Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same α-subunit », Journal of Biological Chemistry, vol. 273, no 42, , p. 27573-27579 (PMID9765290, DOI10.1074/jbc.273.42.27573, lire en ligne)
(en) David O. Lambeth, Kristin N. Tews, Steven Adkins, Dean Frohlich et Barry I. Milavetz, « Expression of Two Succinyl-CoA Synthetases with Different Nucleotide Specificities in Mammalian Tissues », Journal of Biological Chemistry, vol. 279, no 35, , p. 36621-36624 (PMID15234968, DOI10.1074/jbc.M406884200, lire en ligne)
(en) Robert E. Labbe, Takao Kurumada et Jinichi Onisawa, « The role of succinyl-CoA synthetase in the control of heme biosynthesis », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 111, no 2, , p. 403-415 (PMID5879477, DOI10.1016/0304-4165(65)90050-4, lire en ligne)
(en) J. H. Ottaway, J. A. McClellan et C. L. Saunderson, « Succinic thiokinase and metabolic control », International Journal of Biochemistry, vol. 13, no 4, , p. 401-410 (PMID6263728, DOI10.1016/0020-711X(81)90111-7, lire en ligne)
(en) T. M. Jenkins et P. D. Weitzman, « Distinct physiological roles of animal succinate thiokinases Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization », FEBS Letters, vol. 205, no 2, , p. 215-218 (PMID2943604, DOI10.1016/0014-5793(86)80900-0, lire en ligne)
jbc.org
(en) Marie E. Fraser, Koto Hayakawa, Millicent S. Hume, David G. Ryan et Edward R. Brownie, « Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase », Journal of Biological Chemistry, vol. 281, no 16, , p. 11058-11065 (PMID16481318, DOI10.1074/jbc.M511785200, lire en ligne)
(en) James D. Johnson, Wallace W. Muhonen et David O. Lambeth, « Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same α-subunit », Journal of Biological Chemistry, vol. 273, no 42, , p. 27573-27579 (PMID9765290, DOI10.1074/jbc.273.42.27573, lire en ligne)
(en) David O. Lambeth, Kristin N. Tews, Steven Adkins, Dean Frohlich et Barry I. Milavetz, « Expression of Two Succinyl-CoA Synthetases with Different Nucleotide Specificities in Mammalian Tissues », Journal of Biological Chemistry, vol. 279, no 35, , p. 36621-36624 (PMID15234968, DOI10.1074/jbc.M406884200, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) Marie E. Fraser, Koto Hayakawa, Millicent S. Hume, David G. Ryan et Edward R. Brownie, « Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase », Journal of Biological Chemistry, vol. 281, no 16, , p. 11058-11065 (PMID16481318, DOI10.1074/jbc.M511785200, lire en ligne)
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger3 et William T. Wolodko, « A detailed structural description of Escherichia coli succinyl-CoA synthetase », Journal of Molecular Biology, vol. 285, no 4, , p. 1633-1653 (PMID9917402, DOI10.1006/jmbi.1998.2324, lire en ligne)
(en) Jonathan S. Nishimura, « Succinyl-CoA Synthetase Structure-Function Relationships and Other Considerations », Advances in Enzymology and Related Areas of Molecular Biology, vol. 58, , p. 141-172 (PMID3521216, DOI10.1002/9780470123041.ch4, lire en ligne)
(en) William T. Wolodko, Cyril M. Kay et William A. Bridger, « Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli », Biochemistry, vol. 25, no 19, , p. 5420-5425 (PMID3535876, DOI10.1021/bi00367a012, lire en ligne)
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger et William T. Wolodko, « A detailed structural description of Escherichia coli succinly-CoA synthetase », Journal of Molecular Biology, vol. 288, no 3, , p. 501 (PMID10329157, DOI10.1006/jmbi.1999.2773, lire en ligne)
(en) Michael A. Joyce, Marie E. Fraser, Michael N. G. James, William A. Bridger et William T. Wolodko, « ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography », Biochemistry, vol. 39, no 1, , p. 17-25 (PMID10625475, DOI10.1021/bi991696f, lire en ligne)
(en) Isabel Hunger-Glaser, Reto Brun, Markus Linder et Thomas Seebeck, « Inhibition of succinyl CoA synthetase histidine-phosphorylation in Trypanosoma brucei by an inhibitor of bacterial two-component systems », Molecular and Biochemical Parasitology, vol. 100, no 1, , p. 53-59 (PMID10376993, DOI10.1016/S0166-6851(99)00032-8, lire en ligne)
(en) Marie E. Fraser, Michael A. Joyce, David G. Ryan et William T. Wolodko, « Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase », Biochemistry, vol. 41, no 2, , p. 537-546 (PMID11781092, DOI10.1021/bi011518y, lire en ligne)
(en) James D. Johnson, Wallace W. Muhonen et David O. Lambeth, « Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same α-subunit », Journal of Biological Chemistry, vol. 273, no 42, , p. 27573-27579 (PMID9765290, DOI10.1074/jbc.273.42.27573, lire en ligne)
(en) David O. Lambeth, Kristin N. Tews, Steven Adkins, Dean Frohlich et Barry I. Milavetz, « Expression of Two Succinyl-CoA Synthetases with Different Nucleotide Specificities in Mammalian Tissues », Journal of Biological Chemistry, vol. 279, no 35, , p. 36621-36624 (PMID15234968, DOI10.1074/jbc.M406884200, lire en ligne)
(en) Robert E. Labbe, Takao Kurumada et Jinichi Onisawa, « The role of succinyl-CoA synthetase in the control of heme biosynthesis », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 111, no 2, , p. 403-415 (PMID5879477, DOI10.1016/0304-4165(65)90050-4, lire en ligne)
(en) J. H. Ottaway, J. A. McClellan et C. L. Saunderson, « Succinic thiokinase and metabolic control », International Journal of Biochemistry, vol. 13, no 4, , p. 401-410 (PMID6263728, DOI10.1016/0020-711X(81)90111-7, lire en ligne)
(en) T. M. Jenkins et P. D. Weitzman, « Distinct physiological roles of animal succinate thiokinases Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization », FEBS Letters, vol. 205, no 2, , p. 215-218 (PMID2943604, DOI10.1016/0014-5793(86)80900-0, lire en ligne)
(en) S. J. Park, G. Chao et R. P. Gunsalus, « Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter », Journal of Bacteriology, vol. 179, no 13, , p. 4138-4142 (PMID9209026, PMCID179232, lire en ligne)
sciencedirect.com
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger3 et William T. Wolodko, « A detailed structural description of Escherichia coli succinyl-CoA synthetase », Journal of Molecular Biology, vol. 285, no 4, , p. 1633-1653 (PMID9917402, DOI10.1006/jmbi.1998.2324, lire en ligne)
(en) Marie E. Fraser, Michael N.G. James, William A. Bridger et William T. Wolodko, « A detailed structural description of Escherichia coli succinly-CoA synthetase », Journal of Molecular Biology, vol. 288, no 3, , p. 501 (PMID10329157, DOI10.1006/jmbi.1999.2773, lire en ligne)
(en) Isabel Hunger-Glaser, Reto Brun, Markus Linder et Thomas Seebeck, « Inhibition of succinyl CoA synthetase histidine-phosphorylation in Trypanosoma brucei by an inhibitor of bacterial two-component systems », Molecular and Biochemical Parasitology, vol. 100, no 1, , p. 53-59 (PMID10376993, DOI10.1016/S0166-6851(99)00032-8, lire en ligne)
(en) Robert E. Labbe, Takao Kurumada et Jinichi Onisawa, « The role of succinyl-CoA synthetase in the control of heme biosynthesis », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 111, no 2, , p. 403-415 (PMID5879477, DOI10.1016/0304-4165(65)90050-4, lire en ligne)
(en) J. H. Ottaway, J. A. McClellan et C. L. Saunderson, « Succinic thiokinase and metabolic control », International Journal of Biochemistry, vol. 13, no 4, , p. 401-410 (PMID6263728, DOI10.1016/0020-711X(81)90111-7, lire en ligne)
wiley.com
onlinelibrary.wiley.com
(en) Jonathan S. Nishimura, « Succinyl-CoA Synthetase Structure-Function Relationships and Other Considerations », Advances in Enzymology and Related Areas of Molecular Biology, vol. 58, , p. 141-172 (PMID3521216, DOI10.1002/9780470123041.ch4, lire en ligne)
(en) T. M. Jenkins et P. D. Weitzman, « Distinct physiological roles of animal succinate thiokinases Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization », FEBS Letters, vol. 205, no 2, , p. 215-218 (PMID2943604, DOI10.1016/0014-5793(86)80900-0, lire en ligne)