Tsuchiya_2003_Plant.Cell.Physiol_44_96

Reference

Title : Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad - Tsuchiya_2003_Plant.Cell.Physiol_44_96
Author(s) : Tsuchiya T , Suzuki T , Yamada T , Shimada H , Masuda T , Ohta H , Takamiya K
Ref : Plant Cell Physiol , 44 :96 , 2003
Abstract :

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 might be similar to those of serine hydrolases that have a catalytic triad composed of serine, histidine and aspartic acid in their active site. Thus, we introduced mutations into the putative catalytic residue (Ser162) and conserved amino acid residues (histidine, aspartic acid and cysteine) to generate recombinant CaCLH mutants. The three amino acid residues (Ser162, Asp191 and His262) essential for Chlase activity were identified. These results indicate that Chlase is a serine hydrolase and, by analogy with a plausible catalytic mechanism of serine hydrolases, we proposed a mechanism for hydrolysis catalyzed by Chlase.

PubMedSearch : Tsuchiya_2003_Plant.Cell.Physiol_44_96
PubMedID: 12552153
Gene_locus related to this paper: cheal-CACLH

Related information

Gene_locus cheal-CACLH
Family cheal-CACLH    Chlorophyllase_Plant

Citations formats

Tsuchiya T, Suzuki T, Yamada T, Shimada H, Masuda T, Ohta H, Takamiya K (2003)
Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad
Plant Cell Physiol 44 :96

Tsuchiya T, Suzuki T, Yamada T, Shimada H, Masuda T, Ohta H, Takamiya K (2003)
Plant Cell Physiol 44 :96