Yang Wanggui, Cao Yi, Sun Xiaofei, Huang Fei, He Qinghua, Qiao Dairong, Bai Linhan
College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China.
J Basic Microbiol. 2007 Jun;47(3):266-74. doi: 10.1002/jobm.200610263.
The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase (FAD-GPDH), recently reported in plants, has been detailed in yeast and animal systems. It oxidizes glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate (DHAP) on the outer surface of mitochondrial inner membrane. A cDNA encoding the Dunaliella salina mitochondrial glycerol-3-phosphate dehydrogenase (DsFAD-GPDH) has been cloned and sequenced. The full length cDNA is 2791 bp, with an open reading frame (ORF) encoding 650 predicted amino acids, which show strong homology to reported FAD-GPDHs and have an apparent mitochondrial targeting sequence in the N-terminal. The sequence has been submitted to the GenBank database under Accession No. DQ916107. Results of Real-Time Quantitative PCR and enzymatic assays show that expression of DsFAD-GPDH is enhanced at first by salt treatment, and repressed by oxygen deficiency and cold stress.
线粒体FAD依赖的3-磷酸甘油脱氢酶(FAD-GPDH),最近在植物中被报道,已在酵母和动物系统中进行了详细研究。它在线粒体内膜外表面将3-磷酸甘油(G-3-P)氧化为磷酸二羟丙酮(DHAP)。编码盐生杜氏藻线粒体3-磷酸甘油脱氢酶(DsFAD-GPDH)的cDNA已被克隆和测序。全长cDNA为2791 bp,有一个开放阅读框(ORF),编码650个预测的氨基酸,这些氨基酸与已报道的FAD-GPDH有很强的同源性,并且在N端有一个明显的线粒体靶向序列。该序列已提交到GenBank数据库,登录号为DQ916107。实时定量PCR和酶活性分析结果表明,盐处理最初会增强DsFAD-GPDH的表达,而缺氧和冷胁迫则会抑制其表达。