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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...

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Autores principales: Demirev, Atanas V., Khanal, Anamika, Sedai, Bhishma R., Lim, Si Kyu, Na, Min Kyun, Nam, Doo Hyun
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2010
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.
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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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