Bm-iAANAT3: Expression and characterization of a novel arylalkylamine N-acyltransferase from Bombyx mori.

Autor: Battistini MR; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA., O'Flynn BG; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA., Shoji C; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA., Suarez G; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA., Galloway LC; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA., Merkler DJ; Department of Chemistry, University of South Florida, Tampa, FL, 33620, USA. Electronic address: merkler@usf.edu.
Jazyk: angličtina
Zdroj: Archives of biochemistry and biophysics [Arch Biochem Biophys] 2019 Jan; Vol. 661, pp. 107-116. Date of Electronic Publication: 2018 Nov 16.
DOI: 10.1016/j.abb.2018.11.015
Abstrakt: The arylalkylamine N-acyltransferases (AANATs) are enzymes that catalyze the acyl-CoA-dependent formation of N-acylarylalkylamides: acyl-CoA + arylalkylamine → N-acylarylalkylamides + CoA-SH. Herein, we describe our study of a previously uncharacterized AANAT from Bombyx mori: Bm-iAANAT3. Bm-iAANAT3 catalyzes the direct formation of N-acylarylalkylamides and accepts a broad range of short-chain acyl-CoA thioesters and amines as substrates. Acyl-CoA thioesters possessing an acyl chain length >10 carbon atoms are not substrates for Bm-iAANAT3. We report that Bm-iAANAT3 is a "versatile generalist", most likely, functioning in amine acetylation - a reaction in amine inactivation/excretion, cuticle sclerotization, and melanism. We propose a kinetic and chemical mechanism for Bm-iAANAT3 that is consistent with our steady-state kinetic analysis, dead-end inhibition studies, determination of the pH-rate profiles, and site-directed mutagenesis of a catalytically important amino acid in Bm-iAANAT3. These mechanistic studies of Bm-iAANAT3 will foster the development of novel compounds targeted against this enzyme and other insect AANATs for the control of insect pests.
(Copyright © 2018 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: