Unknown

Dataset Information

0

Analysis of genes for succinoyl trehalose lipid production and increasing production in Rhodococcus sp. strain SD-74.


ABSTRACT: Succinoyl trehalose lipids (STLs) are promising glycolipid biosurfactants produced from n-alkanes that are secreted by Rhodococcus species bacteria. These compounds not only exhibit unique interfacial properties but also demonstrate versatile biochemical actions. In this study, three novel types of genes involved in the biosynthesis of STLs, including a putative acyl coenzyme A (acyl-CoA) transferase (tlsA), fructose-bisphosphate aldolase (fda), and alkane monooxygenase (alkB), were identified. The predicted functions of these genes indicate that alkane metabolism, sugar synthesis, and the addition of acyl groups are important for the biosynthesis of STLs. Based on these results, we propose a biosynthesis pathway for STLs from alkanes in Rhodococcus sp. strain SD-74. By overexpressing tlsA, we achieved a 2-fold increase in the production of STLs. This study advances our understanding of bacterial glycolipid production in Rhodococcus species.

SUBMITTER: Inaba T 

PROVIDER: S-EPMC3811520 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Analysis of genes for succinoyl trehalose lipid production and increasing production in Rhodococcus sp. strain SD-74.

Inaba Tomohiro T   Tokumoto Yuta Y   Miyazaki Yusuke Y   Inoue Naoyuki N   Maseda Hideaki H   Nakajima-Kambe Toshiaki T   Uchiyama Hiroo H   Nomura Nobuhiko N  

Applied and environmental microbiology 20130913 22


Succinoyl trehalose lipids (STLs) are promising glycolipid biosurfactants produced from n-alkanes that are secreted by Rhodococcus species bacteria. These compounds not only exhibit unique interfacial properties but also demonstrate versatile biochemical actions. In this study, three novel types of genes involved in the biosynthesis of STLs, including a putative acyl coenzyme A (acyl-CoA) transferase (tlsA), fructose-bisphosphate aldolase (fda), and alkane monooxygenase (alkB), were identified.  ...[more]

Similar Datasets

| S-EPMC4429620 | biostudies-literature
| S-EPMC197028 | biostudies-other
| S-EPMC7953298 | biostudies-literature
| S-EPMC3294463 | biostudies-literature
| S-EPMC92901 | biostudies-literature
| S-EPMC374424 | biostudies-literature
| S-EPMC167480 | biostudies-other
2024-05-22 | PXD044565 | Pride
| S-EPMC5383884 | biostudies-literature
| S-EPMC126766 | biostudies-literature