Succinyl-CoA synthetase

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

3D structures of succinyl-CoA synthetase

Updated on 20-September-2018

Additional Resources

References

  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]

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