Open AccessStudies on the re ‐Citrate Synthase Reaction
Author(s) -
Gottschalk Gerhard,
Dittbrenner Susanne,
Lenz Helmut,
Eggerer Hermann
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01787.x
Subject(s) - citrate synthase , atp citrate lyase , chemistry , stereospecificity , enzyme , atp synthase , biochemistry , stereochemistry , catalysis
re ‐Citrate synthase catalyzes the hydrolysis of R ‐citryl‐CoA and R ‐malyl‐CoA. The S diastereomers are not attacked. The stereospecificity of the hydrolase activity is an agreement with the stereochemical course of citrate synthesis as catalyzed by this enzyme. The cooperative action of 2‐oxoglutarate and metal ions (Co 2+ ) induces maximum acetyl‐CoA enolase activity of re ‐citrate synthase. R ‐Malate is not effective in this reaction. Since S ‐malate is the best inducer of the enolase activity of si ‐citrate synthase this suggests differences in the architecture of the active sites of these enzymes. When re ‐citrate synthase is incubated with citrate and coenzyme A in tritiated water, tritium is incorporated into citrate. This indicates that the re ‐citrate synthase reaction is reversible.