Li_2016_Biochem.Biophys.Res.Commun_474_226

Reference

Title : Crystal structure of methylesterase family member 16 (MES16) from Arabidopsis thaliana - Li_2016_Biochem.Biophys.Res.Commun_474_226
Author(s) : Li H , Pu H
Ref : Biochemical & Biophysical Research Communications , 474 :226 , 2016
Abstract :

Methylesterase family member 16 (MES16) is an integral component of chlorophyll breakdown. It catalyzes the demethylation of fluorescent chlorophyll catabolite (FCC) and pheophorbide in vitro, and specifically demethylates FCC in vivo. Here we report the crystal structure of MES16 from Arabidopsis thaliana at 2.8 A resolution. The structure confirm that MES16 is a member of the alpha/beta-hydrolase superfamily with Ser-87, His-239, and Asp-211 as the catalytic triad. Our biochemical studies reveal that MES16 has esterase activity with methyl-indole acetic acid as the substrate, and the catalytically essential role of Ser-87 has been demonstrated.

PubMedSearch : Li_2016_Biochem.Biophys.Res.Commun_474_226
PubMedID: 27109476
Gene_locus related to this paper: arath-AT4G16690

Related information

Substrate MeJA    MeIAA
Gene_locus arath-AT4G16690
Structure 5HK8

Citations formats

Li H, Pu H (2016)
Crystal structure of methylesterase family member 16 (MES16) from Arabidopsis thaliana
Biochemical & Biophysical Research Communications 474 :226

Li H, Pu H (2016)
Biochemical & Biophysical Research Communications 474 :226