Title : Serine carboxypeptidase-like acyltransferases - Milkowski_2004_Phytochemistry_65_517
Author(s) : Milkowski C , Strack D
Ref : Phytochemistry , 65 :517 , 2004
Abstract :

In plant secondary metabolism, an alternative pathway of ester formation is facilitated by acyltransferases accepting 1-O-beta-acetal esters (1-O-beta-glucose esters) as acyl donors instead of coenzyme A thioesters. Molecular data indicate homology of these transferases with hydrolases of the serine carboxypeptidase type defining them as serine carboxypeptidase-like (SCPL) acyltransferases. During evolution, they apparently have been recruited from serine carboxypeptidases and adapted to take over acyl transfer function. SCPL acyltransferases belong to the highly divergent class of alpha/beta hydrolases. These enzymes make use of a catalytic triad formed by a nucleophile, an acid and histidine acting as a charge relay system for the nucleophilic attack on amide or ester bonds. In analogy to SCPL acyltransferases, bacterial thioesterase domains are known which favour transferase activity over hydrolysis. Structure elucidation reveals water exclusion and a distortion of the oxyanion hole responsible for the changed activity. In plants, SCPL proteins form a large family. By sequence comparison, a distinguished number of Arabidopsis SCPL proteins cluster with proven SCPL acyltransferases. This indicates the occurrence of a large number of SCPL proteins co-opted to catalyse acyltransfer reactions. SCPL acyltransferases are ideal systems to investigate principles of functional adaptation and molecular evolution of plant genes.

PubMedSearch : Milkowski_2004_Phytochemistry_65_517
PubMedID: 15003414
Gene_locus related to this paper: arath-SCP8

Related information

Gene_locus arath-SCP8
Family arath-SCP8    Carboxypeptidase_S10

Citations formats

Milkowski C, Strack D (2004)
Serine carboxypeptidase-like acyltransferases
Phytochemistry 65 :517

Milkowski C, Strack D (2004)
Phytochemistry 65 :517