Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity

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dc.contributor.author Nikolau, Basil
dc.contributor.author Yandeau-Nelson, Marna
dc.contributor.author Jing, Fuyuan
dc.contributor.author Cantu, David
dc.contributor.author Reilly, Peter
dc.contributor.author Tvaruzkova, Jarmila
dc.contributor.author Chipman, Jay
dc.contributor.author Nikolau, Basil
dc.contributor.author Yandeau-Nelson, Marna
dc.contributor.author Reilly, Peter
dc.contributor.department Chemical and Biological Engineering
dc.date 2019-06-30T08:41:00.000
dc.date.accessioned 2020-06-30T01:09:27Z
dc.date.available 2020-06-30T01:09:27Z
dc.date.copyright Sat Jan 01 00:00:00 UTC 2011
dc.date.embargo 2012-11-09
dc.date.issued 2011-08-10
dc.description.abstract <p><strong>Background:</strong> Acyl-acyl carrier protein thioesterases (acyl-ACP TEs) catalyze the hydrolysis of the thioester bond that links the acyl chain to the sulfhydryl group of the phosphopantetheine prosthetic group of ACP. This reaction terminates acyl chain elongation of fatty acid biosynthesis, and in plant seeds it is the biochemical determinant of the fatty acid compositions of storage lipids.</p> <p><strong>Results:</strong> To explore acyl-ACP TE diversity and to identify novel acyl ACP-TEs, 31 acyl-ACP TEs from wide-ranging phylogenetic sources were characterized to ascertain their in vivo activities and substrate specificities. These acylACP TEs were chosen by two different approaches: 1) 24 TEs were selected from public databases on the basis of phylogenetic analysis and fatty acid profile knowledge of their source organisms; and 2) seven TEs were molecularly cloned from oil palm (Elaeis guineensis), coconut (Cocos nucifera) and Cuphea viscosissima, organisms that produce medium-chain and short-chain fatty acids in their seeds. The in vivo substrate specificities of the acylACP TEs were determined in E. coli. Based on their specificities, these enzymes were clustered into three classes: 1) Class I acyl-ACP TEs act primarily on 14- and 16-carbon acyl-ACP substrates; 2) Class II acyl-ACP TEs have broad substrate specificities, with major activities toward 8- and 14-carbon acyl-ACP substrates; and 3) Class III acyl-ACP TEs act predominantly on 8-carbon acyl-ACPs. Several novel acyl-ACP TEs act on short-chain and unsaturated acylACP or 3-ketoacyl-ACP substrates, indicating the diversity of enzymatic specificity in this enzyme family.</p> <p><strong>Conclusion:</strong> These acyl-ACP TEs can potentially be used to diversify the fatty acid biosynthesis pathway to produce novel fatty acids.</p>
dc.description.comments <p>Published in BMC Biochemistry 12 (2011): 44. doi:<a href="http://dx.doi.org/10.1186/1471-2091-12-44" target="_blank">10.1186/1471-2091-12-44</a>.</p>
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dc.identifier archive/lib.dr.iastate.edu/cbe_pubs/3/
dc.identifier.articleid 1003
dc.identifier.contextkey 3459135
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath cbe_pubs/3
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/13395
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/cbe_pubs/3/1471_2091_12_44.pdf|||Fri Jan 14 23:16:16 UTC 2022
dc.source.uri 10.1186/1471-2091-12-44
dc.subject.disciplines Biochemical and Biomolecular Engineering
dc.subject.disciplines Biological Engineering
dc.title Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 73b33082-7300-4c56-8019-d5e13b9898de
relation.isAuthorOfPublication 0559572a-07dd-4c7c-92fe-b7c1aa1ad253
relation.isAuthorOfPublication 0727532a-2892-42e2-84ab-5af5088f76c6
relation.isOrgUnitOfPublication 86545861-382c-4c15-8c52-eb8e9afe6b75
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