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Arabidopsis acyl-acyl carrier protein synthetase AAE15 with medium chain fatty acid specificity is functional in cyanobacteria
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology. Georg-August-University, Germany.
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0003-1899-7649
2016 (English)In: AMB Express, ISSN 2191-0855, E-ISSN 2191-0855, Vol. 6, no 1, 1-9 p., 7Article in journal (Refereed) Published
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Abstract [en]

Cyanobacteria are potential hosts for the biosynthesis of oleochemical compounds. The metabolic precursors for such compounds are fatty acids and their derivatives, which require chemical activation to become substrates in further conversion steps. We characterized the acyl activating enzyme AAE15 of Arabidopsis encoded by At4g14070, which is a homologue of a cyanobacterial acyl-ACP synthetase (AAS). We expressed AAE15 in insect cells and demonstrated its AAS activity with medium chain fatty acid (C10-C14) substrates in vitro. Furthermore, we used AAE15 to complement a Synechocystis aas deletion mutant and showed that the new strain preferentially incorporates supplied medium chain fatty acids into internal lipid molecules. Based on this data we propose that AAE15 can be utilized in metabolic engineering strategies for cyanobacteria that aim to produce compounds based on medium chain fatty acids.

Place, publisher, year, edition, pages
BioMed Central, 2016. Vol. 6, no 1, 1-9 p., 7
Keyword [en]
Acyl-ACP synthetase, Medium chain fatty acids, Arabidopsis, Cyanobacteria
National Category
Medical Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-182150DOI: 10.1186/s13568-016-0178-zISI: 000368761900001PubMedID: 26797881Scopus ID: 2-s2.0-84955069324OAI: oai:DiVA.org:kth-182150DiVA: diva2:904963
Note

QC 20160220

Available from: 2016-02-20 Created: 2016-02-16 Last updated: 2016-02-20Bibliographically approved

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CiteExportLink to record
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