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Functional and structural characterization of a novel catechol‐ O ‐methyltransferase from Schizosaccharomyces pombe
Author(s) -
Wang Qing,
Teng Maikun,
Li Xu
Publication year - 2019
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1977
Subject(s) - schizosaccharomyces pombe , catechol o methyl transferase , methyltransferase , mutagenesis , biochemistry , catechol , enzyme , schizosaccharomyces , biology , chemistry , o methyltransferase , yeast , stereochemistry , genetics , saccharomyces cerevisiae , mutation , gene , methylation , genotype
Catechol‐ O ‐methyltransferase (COMT 1 ) catalyzes the transfer of a methyl group from S‐adenosylmethionine (SAM) to various catechol substrates. COMTs play vital roles in physiological processes in animals, plants, and fungi, as well as bacteria, and have essential application values in industry. sp COMT is a probable COMT from Schizosaccharomyces pombe . It has an extraordinary intracellular distribution different from other homologs and would thus be predicted to perform a distinct physiological function. In this report, recombinant sp COMT was purified and kinetically characterized for the first time. The enzymology assays indicate that sp COMT is a metal‐dependent enzyme and belongs to class I OMTs. In addition, the crystal structures of apo‐ sp COMT and SAM‐complexed sp COMT were also presented, revealing that sp COMT possesses a conserved SAM‐binding site and Mg 2+ pocket, but a distinct substrate pocket was not present in homologs. The mutagenesis ITC analysis revealed the SAM recognition characteristics of sp COMT. Based on all of the above findings, we speculated about the putative substrates’ characteristics and the substrate recognition mechanisms of sp COMT. This work will help in elucidating the physiological functions of sp COMT in S. pombe . © 2018 IUBMB Life, 71(3):330–339, 2019