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The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini
Streptomyces toxytricini produces lipstatin, a specific inhibitor of pancreatic lipase, which is derived from two fatty acid moieties with eight and 14 carbon atoms. The pccB gene locus in 10.6 kb fragment of S. toxytricini chromosomal DNA contains three genes for acyl-coenzyme A carboxylase (ACCase...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Springer-Verlag
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886142/ https://www.ncbi.nlm.nih.gov/pubmed/20437235 http://dx.doi.org/10.1007/s00253-010-2587-2 |
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author | Demirev, Atanas V. Khanal, Anamika Sedai, Bhishma R. Lim, Si Kyu Na, Min Kyun Nam, Doo Hyun |
author_facet | Demirev, Atanas V. Khanal, Anamika Sedai, Bhishma R. Lim, Si Kyu Na, Min Kyun Nam, Doo Hyun |
author_sort | Demirev, Atanas V. |
collection | PubMed |
description | Streptomyces toxytricini produces lipstatin, a specific inhibitor of pancreatic lipase, which is derived from two fatty acid moieties with eight and 14 carbon atoms. The pccB gene locus in 10.6 kb fragment of S. toxytricini chromosomal DNA contains three genes for acyl-coenzyme A carboxylase (ACCase) complex accA3, pccB, and pccE that are presumed to be involved in secondary metabolism. The pccB gene encoding a β subunit of ACCase [carboxyltransferase (CT)] was identified upstream of pccE gene for a small protein of ε subunit. The accA3 encoding the α subunit of ACCase [biotin carboxylase (BC)] was also identified downstream of pccB gene. When the pccB and pccE genes were inactivated by homologous recombination, the lipstatin production was reduced as much as 80%. In contrast, the accumulation of another compound, tetradeca-5.8-dienoic acid (the major lipstatin precursor), was 4.5-fold increased in disruptant compared with wild-type. It implies that PccB of S. toxytricini is involved in the activation of octanoic acid to hexylmalonic acid for lipstatin biosynthesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00253-010-2587-2) contains supplementary material, which is available to authorized users. |
format | Text |
id | pubmed-2886142 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-28861422010-07-21 The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini Demirev, Atanas V. Khanal, Anamika Sedai, Bhishma R. Lim, Si Kyu Na, Min Kyun Nam, Doo Hyun Appl Microbiol Biotechnol Applied Microbial and Cell Physiology Streptomyces toxytricini produces lipstatin, a specific inhibitor of pancreatic lipase, which is derived from two fatty acid moieties with eight and 14 carbon atoms. The pccB gene locus in 10.6 kb fragment of S. toxytricini chromosomal DNA contains three genes for acyl-coenzyme A carboxylase (ACCase) complex accA3, pccB, and pccE that are presumed to be involved in secondary metabolism. The pccB gene encoding a β subunit of ACCase [carboxyltransferase (CT)] was identified upstream of pccE gene for a small protein of ε subunit. The accA3 encoding the α subunit of ACCase [biotin carboxylase (BC)] was also identified downstream of pccB gene. When the pccB and pccE genes were inactivated by homologous recombination, the lipstatin production was reduced as much as 80%. In contrast, the accumulation of another compound, tetradeca-5.8-dienoic acid (the major lipstatin precursor), was 4.5-fold increased in disruptant compared with wild-type. It implies that PccB of S. toxytricini is involved in the activation of octanoic acid to hexylmalonic acid for lipstatin biosynthesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00253-010-2587-2) contains supplementary material, which is available to authorized users. Springer-Verlag 2010-05-02 2010 /pmc/articles/PMC2886142/ /pubmed/20437235 http://dx.doi.org/10.1007/s00253-010-2587-2 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Applied Microbial and Cell Physiology Demirev, Atanas V. Khanal, Anamika Sedai, Bhishma R. Lim, Si Kyu Na, Min Kyun Nam, Doo Hyun The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title | The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title_full | The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title_fullStr | The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title_full_unstemmed | The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title_short | The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini |
title_sort | role of acyl-coenzyme a carboxylase complex in lipstatin biosynthesis of streptomyces toxytricini |
topic | Applied Microbial and Cell Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886142/ https://www.ncbi.nlm.nih.gov/pubmed/20437235 http://dx.doi.org/10.1007/s00253-010-2587-2 |
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