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
Author(s)
남두현데미레프아타나스아나미까 커널[아나미까 커널]비시머 세다이[비시머 세다이]임시규[임시규]나민균
Keywords
LIPASE INHIBITOR LIPSTATIN; COA CARBOXYLASE; ESCHERICHIA-COLI; COELICOLOR A3(2); MYCOBACTERIUM-TUBERCULOSIS; PANCREATIC LIPASE; CONJUGAL TRANSFER; A CARBOXYLASE; GENE-CLUSTER; IDENTIFICATION
Issue Date
201006
Publisher
SPRINGER
Citation
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.87, no.3, pp.1129 - 1139
Abstract
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 beta subunit of ACCase [carboxyltransferase (CT)] was identified upstream of pccE gene for a small protein of epsilon subunit. The accA3 encoding the alpha 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.
URI
http://hdl.handle.net/YU.REPOSITORY/22393http://dx.doi.org/10.1007/s00253-010-2587-2
ISSN
0175-7598
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약학대학 > 약학부 > Articles
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