Article
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 - 15 Jan 2002
Fraser Marie E, Joyce Michael A, Ryan David G, Wolodko William T
Abstract excerpt
Succinyl-CoA synthetase catalyzes the reversible reaction succinyl-CoA + NDP + P(i) <--> succinate + CoA + NTP (N denoting adenosine or guanosine). The enzyme consists of two different subunits, designated alpha and beta. During the reaction, a histidine residue of the alpha-subunit is transiently phosphorylated. This histidine residue interacts with Glu 208 alpha at site I in the structures of phosphorylated and...
Topics
- Adenosine
- Alanine
- Aspartic Acid
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Glutamic Acid
- Histidine
- Hydrogen Bonding
- Kinetics