Acyltransferase families that act on thioesters: Sequences, structures, and mechanisms

Author:

de Carvalho Caio C.1,Murray Ian P.1,Nguyen Hung2,Nguyen Tin12,Cantu David C.1ORCID

Affiliation:

1. Department of Chemical and Materials Engineering University of Nevada, Reno Reno Nevada USA

2. Department of Computer Science and Software Engineering Auburn University Auburn Alabama USA

Abstract

AbstractAcyltransferases (AT) are enzymes that catalyze the transfer of acyl group to a receptor molecule. This review focuses on ATs that act on thioester‐containing substrates. Although many ATs can recognize a wide variety of substrates, sequence similarity analysis allowed us to classify the ATs into fifteen distinct families. Each AT family is originated from enzymes experimentally characterized to have AT activity, classified according to sequence similarity, and confirmed with tertiary structure similarity for families that have crystallized structures available. All the sequences and structures of the AT families described here are present in the thioester‐active enzyme (ThYme) database. The AT sequences and structures classified into families and available in the ThYme database could contribute to enlightening the understanding acyl transfer to thioester‐containing substrates, most commonly coenzyme A, which occur in multiple metabolic pathways, mostly with fatty acids.

Funder

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

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