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Acyltransferase families that act on thioesters: Sequences,structures, and mechanisms |
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| Authors: | Caio C. de Carvalho Ian P. Murray Hung Nguyen Tin Nguyen David C. Cantu |
| Affiliation: | 1. Department of Chemical and Materials Engineering, University of Nevada, Reno, Reno, Nevada, USA Contribution: Investigation, Writing - original draft, Methodology, Validation, Writing - review & editing, Formal analysis, Supervision, Data curation, Conceptualization, Visualization;2. Department of Chemical and Materials Engineering, University of Nevada, Reno, Reno, Nevada, USA Contribution: Methodology, Validation, Visualization, Formal analysis, Writing - review & editing;3. Department of Computer Science and Software Engineering, Auburn University, Auburn, Alabama, USA Contribution: Data curation, Writing - review & editing;4. Department of Chemical and Materials Engineering, University of Nevada, Reno, Reno, Nevada, USA Department of Computer Science and Software Engineering, Auburn University, Auburn, Alabama, USA Contribution: Funding acquisition, Writing - review & editing, Supervision;5. Department of Chemical and Materials Engineering, University of Nevada, Reno, Reno, Nevada, USA |
| Abstract: | Acyltransferases (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. |
| Keywords: | acyltransferases coenzyme A enzyme families enzyme structures |