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Investigation of amino acid residues involved in the sunflower thiolase reaction mechanism
Author(s) -
Cadet Melissa,
Gomez Iris,
Dyer James H.
Publication year - 2009
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.23.1_supplement.502.14
Subject(s) - thiolase , sunflower , histidine , biochemistry , chemistry , cysteine , mutagenesis , active site , amino acid , substrate (aquarium) , mechanism (biology) , enzyme , biology , mutation , gene , ecology , philosophy , epistemology , 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. 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. The purpose of this research is to do site‐directed mutagenesis of the corresponding cysteine and histidine residues in the sunflower acetoacetyl CoA thiolase