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Investigation of Mutations of Sunflower Cotyledon Acetoacetyl CoA Thiolase
Author(s) -
Cadet Melissa,
Gomez Iris,
Schiedel Anke C.,
Oeljeklaus Silke,
Dyer James H.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.896.2
Subject(s) - thiolase , sunflower , mutagenesis , histidine , biochemistry , active site , chemistry , substrate (aquarium) , amino acid , enzyme , biology , mutation , gene , ecology , agronomy , dehydrogenase
Acetoacetyl CoA thiolase is one of two thiolase activities found in sunflower cotyledons. This thiolase activity is involved in the oxidation of the short‐chain substrate acetoacetyl CoA to produce two acetyl CoAs and also has been characterized as a synthetic thiolase via the formation of acetoacetyl CoA from two acetyl CoAs. Crystal structures of thiolase from other organisms have identified conserved cysteines and a histidine present in the active site of the enzyme indicating that these residues probably play a key role in the reaction mechanism and other residues have been implicated in the stabilization of the enolate intermediate in the synthetic reaction. Site‐directed mutagenesis of the various amino acid residues was done and the effect of these mutations on the catalytic activity was measured.