期刊名称：International Journal of Environmental Science and Development
印刷版ISSN：2010-0264
出版年度：2014
卷号：5
期号：4
页码：362-366
DOI：10.7763/IJESD.2014.V5.510
摘要：Acetoacetyl-CoA thiolase (AACT, β-ketothiolase) is an enzyme that catalyzes the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA.In plants, AACT is known to be involved in the early step of mevalonate pathway which is essential in producing isoprenoid compounds such as sterols, carotenoids and growth regulators.In order to study this gene, we attempt to clone the gene from oil palm.The AACT gene was cloned from a genomic library of oil palm using a homologous probe from the AACT cDNA clone.The probe is consisted of 1.5 kb in length.A fragment of 12 470 bp was successfully sequenced and contains nine exons interrupted by eight introns.This fragment represented 886 bp in length or 59 % of 1247 bp of the putative AACT mRNA sequence.Transcription start site (TSS) and its regulatory regions were predicted at the 5’-flanking region of this gene.Three TSS points, at positions -1284, -1283 and -280 from the putative start codon were identified.The binding sites for GT-1 element, SBF-1 and sequences resembling the binding sites of several other transcription factors were also identified.
关键词：β-ketothiolase; enzyme; mevalonate pathway; polyhydrohybutyrate (PHB); regulatory regions
