Succinyl-CoA synthetase

From Proteopedia

Jump to: navigation, search

E. coli succinyl-CoA synthetase α subunit (grey, yellow) and β subunit (green, magenta) complex with CoA and phosphate (PDB code 1cqj)

Drag the structure with the mouse to rotate

Additional Resources


  1. Joyce MA, Fraser ME, Brownie ER, James MN, Bridger WA, Wolodko WT. Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetase. Biochemistry. 1999 Jun 1;38(22):7273-83. PMID:10353839 doi:10.1021/bi990527s
  2. Fraser ME, Joyce MA, Ryan DG, Wolodko WT. Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase. Biochemistry. 2002 Jan 15;41(2):537-46. PMID:11781092
  3. Bild GS, Janson CA, Boyer PD. Subunit interaction during catalysis. ATP modulation of catalytic steps in the succinyl-CoA synthetase reaction. J Biol Chem. 1980 Sep 10;255(17):8109-15. PMID:6997289
  4. Mikeladze DG, Matveeva LN, Severin SE. [Reaction mechanism of succinyl CoA synthetase from pigeon thoracic muscle] Biokhimiia. 1978 Aug;43(8):1458-67. PMID:570066
  5. Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT. ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography. Biochemistry. 2000 Jan 11;39(1):17-25. PMID:10625475
  6. Frank J. Moffet and W. A. Bridger. The Kinetics of Succinyl Coenzyme A Synthetase from Escherichia coli : A REACTION WITH A COVALENT ENZYME-SUBSTRATE INTERMEDIATE NOT EXHIBITING "PING-PONG" KINETICS J. Biol. Chem. 1970 245: 2758-2762.[1]
  7. Um, H.-D., and C. Klein. 1993. Evidence for allosteric regulation of succinyl-CoA synthetase. Biochem. J. 295:821–826.[2]

Content Donators

Personal tools