Ponomarev A G, Bubiakina V V, Tatarinova T D, Zelenin S M
Institute for Biological Problems of Cryolithozone, Siberian Branch, Russian Academy of Sciences, Yakutsk.
Tsitologiia. 1998;40(6):579-84.
Two degenerate oligonucleotide sequence primers and polymerase chain reactions on total DNA have been utilized to clone on 651--bp gene fragment coding the central part of amino acid sequence of an earlier unknown aldehyde dehydrogenase (ALDH) from mung bean. The deduced partial amino acid sequence for this aldehyde dehydrogenase shows about 65% sequence identity to ALDHs of Vibrio cholerae Rhodococcus sp., Alcaligenes eutrophus and about 45% sequence identity to mammalian ALDHs 1 and 2, ALDHs of Aspergillus niger and A, nidulans, the betain aldehyde dehydrogenase from spinach. Alignment of the mung bean aldehyde dehydrogenase partial amino acid sequence with the sequence of 16 NAD(P)(+)-dependent aldehyde dehydrogenases has demonstrated that all strictly conserved amino acid residues and all three conservative regions are identical.
利用两个简并寡核苷酸序列引物和对总DNA进行聚合酶链反应,克隆了一个651bp的基因片段,该片段编码绿豆中一种此前未知的醛脱氢酶(ALDH)氨基酸序列的中央部分。推导得到的该醛脱氢酶部分氨基酸序列与霍乱弧菌、红球菌属、嗜碱产碱菌的醛脱氢酶显示出约65%的序列同一性,与哺乳动物醛脱氢酶1和2、黑曲霉和构巢曲霉的醛脱氢酶、菠菜的甜菜碱醛脱氢酶显示出约45%的序列同一性。绿豆醛脱氢酶部分氨基酸序列与16种NAD(P)(+)依赖性醛脱氢酶的序列比对表明,所有严格保守的氨基酸残基和所有三个保守区域都是相同的。