FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp PCC 6803

doi:10.1080/21655979.2017.1317574

	FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp PCC 6803
	Zhang, Haowei 1; Liu, Yinghui 2; Yao, Changhong 3; Cao, Xupeng 2; Tian, Jing 1; Xue, Song 2
刊名	BIOENGINEERED
	2017
卷号	8 期号:6 页码:707-715
关键词	Beta-ketoacyl-acp Reductase Acetoacetyl-coa Reductase Poly-3-hydroxybutyrate Fatty Acid Synechocystis
ISSN号	2165-5979
DOI	10.1080/21655979.2017.1317574
文献子类	Article
英文摘要	The production of poly-3-hydroxybutyrate (PHB) by photosynthetic cyanobacteria is a potentially sustainable production method for the biodegradable plastics industry. beta-Ketoacyl-ACP reductase (FabG), from the photosynthetic cyanobacterium Synechocystis sp. PCC 6803 (SpFabG), is the first NADPH-dependent reductase in the fatty acid biosynthesis pathway. Its structure is similar to that of acetoacetyl-CoA reductase (SpPhaB), which is critical for PHB synthesis and can replace SpPhaB for acetoacetyl-CoA reduction in vitro. However, the specific function of SpFabG in fatty acid synthesis and whether SpFabG could participate in PHB synthesis in vivo were not yet clear. In this study, the role of SpFabG in fatty acid synthesis was first verified in vivo by knocking down and overexpressing of fabG. It was shown that SpFabG was essential yet not rate-limiting for fatty acid biosynthesis. The biochemical characterization of SpFabG using acetoacetyl-CoA as the substrate showed that the optimum temperature, optimum pH, Km and kcat were 30 degrees C, 7, 2.30 mM, and 19.85 s(-1), respectively, which exemplified the ability of SpFabG to reduce acetoacetyl-CoA with a relatively low affinity and weak catalytic efficiency. Functional analysis of SpFabG in vivo indicated that SpFabG was able to partially complement SpPhaB under nitrogen-deprived conditions, and overexpression of fabG led to the diversion of partial carbon flux from fatty acid toward PHB synthesis.
WOS关键词	CARRIER PROTEIN REDUCTASE ; POLY-BETA-HYDROXYBUTYRATE ; KETOACYL-ACP REDUCTASE ; FATTY-ACID SYNTHASE ; ESCHERICHIA-COLI ; PLASMODIUM-FALCIPARUM ; NITROGEN-STARVATION ; SP PCC-6803 ; GENES ; ACCUMULATION
WOS研究方向	Biotechnology & Applied Microbiology
语种	英语
出版者	TAYLOR & FRANCIS INC
WOS记录号	WOS:000423226100005
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/168582]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
通讯作者	Cao, Xupeng; Tian, Jing; Xue, Song
作者单位	1.Dalian Polytech Univ, Sch Engn, Dalian, Liaoning, Peoples R China 2.Chinese Acad Sci, Marine Bioengn Grp, Dalian Inst Chem Phys, Dalian, Peoples R China 3.Sichuan Univ, Dept Pharmaceut & Biol Engn, Sch Chem Engn, Chengdu, Sichuan, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Haowei,Liu, Yinghui,Yao, Changhong,et al. FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp PCC 6803[J]. BIOENGINEERED,2017,8(6):707-715.
APA	Zhang, Haowei,Liu, Yinghui,Yao, Changhong,Cao, Xupeng,Tian, Jing,&Xue, Song.(2017).FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp PCC 6803.BIOENGINEERED,8(6),707-715.
MLA	Zhang, Haowei,et al."FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp PCC 6803".BIOENGINEERED 8.6(2017):707-715.