Article
Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad.
Plant & cell physiology - 1 Jan 2003
Tsuchiya Tohru, Suzuki Takuo, Yamada Takafumi, Shimada Hiroshi, Masuda Tatsuru, Ohta Hiroyuki, Takamiya Ken-ichiro
Abstract excerpt
Chlorophyllases (Chlases), cloned so far, contain a lipase motif with the active serine residue of the catalytic triad of triglyceride lipases. Inhibitors specific for the catalytic serine residue in serine hydrolases, which include lipases effectively inhibited the activity of the recombinant Chenopodium album Chlase (CaCLH). From this evidence we assumed that the catalytic mechanism of hydrolysis by Chlase...
Topics
- Amino Acid Sequence
- Aspartic Acid
- Binding Sites
- Carboxylic Ester Hydrolases
- Catalysis
- Chenopodium album
- Enzyme Inhibitors
- Histidine
- Hydrolysis
- Isoflurophate
- Lipase
- Molecular Sequence Data
- Morpholines
- Mutagenesis, Site-Directed