de Vet E C, Prinsen H C, van den Bosch H
Centre for Biomembranes and Lipid Enzymology, Utrecht University, The Netherlands.
Biochem Biophys Res Commun. 1998 Jan 14;242(2):277-81. doi: 10.1006/bbrc.1997.7950.
The nucleotide sequence is reported of a cDNA clone encoding a Caenorhabditis elegans homolog of guinea pig and human alkyl-dihydroxyacetonephosphate synthase. The open reading frame encodes a protein of 597 amino acids which shows extensive homology with the mammalian enzymes (52% identical and about 76% similar in the overlapping region). In contrast to the mammalian enzymes, which carry a consensus peroxisomal targeting signal type 2 in a cleavable N-terminal presequence, this Caenorhabditis elegans homolog carries a consensus peroxisomal targeting signal type 1 (CKL) at its C-terminus. Expression of this protein in an in vitro transcription/translation system yielded a 65 kDa protein. Recombinant aenorhabditis elegans alkyl-DHAP synthase expressed in the yeast Pichia pastoris was enzymatically active.
报道了一个编码秀丽隐杆线虫中豚鼠和人烷基二羟基丙酮磷酸合酶同源物的cDNA克隆的核苷酸序列。该开放阅读框编码一个597个氨基酸的蛋白质，它与哺乳动物的酶具有广泛的同源性（在重叠区域52%相同且约76%相似）。与哺乳动物的酶不同，哺乳动物的酶在可切割的N端前序列中带有一个2型过氧化物酶体靶向信号共识序列，而这个秀丽隐杆线虫同源物在其C端带有一个1型过氧化物酶体靶向信号共识序列（CKL）。该蛋白在体外转录/翻译系统中的表达产生了一个65 kDa的蛋白。在酵母毕赤酵母中表达的重组秀丽隐杆线虫烷基 - DHAP合酶具有酶活性。
