Crystallization of succinyl-CoA synthetase from Escherichia coli.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference19 articles.
1. A phosphorus 31 nuclear magnetic resonance study of the intermediates of the Escherichia coli succinyl coenzyme A synthetase reaction. Evidence for substrate synergism and catalytic cooperativity.
2. Evidence for two types of subunits in succinyl coenzyme a synthetase
3. Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl coenzyme A synthetase.
4. Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli.
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1. Novel Characteristics of Succinate Coenzyme A (Succinate-CoA) Ligases: Conversion of Malate to Malyl-CoA and CoA-Thioester Formation of Succinate Analogues In Vitro;Applied and Environmental Microbiology;2014-01
2. Succinyl-CoA Synthetase Structure-Function Relationships and Other Considerations;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. 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;2001-12-14
4. Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase;Journal of Molecular Biology;2000-06
5. ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography,;Biochemistry;1999-12-09
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