Kim N S, Umezawa Y, Ohmura S, Kato S
Kanagawa Academy of Science and Technology (KAST), Japan.
J Biol Chem. 1993 May 25;268(15):11217-21.
Glyoxalase I (EC 4.4.1.5) catalyzes the transformation of methylglyoxal and glutathione to S-lactoylglutathione. We have isolated human cDNA clones encoding glyoxalase I from a phorbol myristate acetate-treated U937 cDNA library. This cDNA encodes a protein of 184 amino acids with a calculated M(r) of 20,719. The amino acid composition calculated from the deduced amino acid sequence agreed with that reported for glyoxalase I purified from human erythrocytes. The Escherichia coli cells carrying the expression vector of this cDNA acquired methylglyoxal resistance and the cell lysate showed the high activity of glyoxalase I. The amino acid sequence of human glyoxalase I exhibited 57% identity with Pseudomonas putida glyoxalase I at the C-terminal two-thirds, suggesting that the two enzymes may have originated from a common ancestor.
乙二醛酶I（EC 4.4.1.5）催化甲基乙二醛和谷胱甘肽转化为S-乳酰谷胱甘肽。我们从佛波酯肉豆蔻酸酯乙酸盐处理的U937 cDNA文库中分离出编码乙二醛酶I的人cDNA克隆。该cDNA编码一种由184个氨基酸组成的蛋白质，计算所得的分子量（M(r)）为20,719。根据推导的氨基酸序列计算出的氨基酸组成与从人红细胞中纯化得到的乙二醛酶I的报道结果一致。携带该cDNA表达载体的大肠杆菌细胞获得了对甲基乙二醛的抗性，并且细胞裂解物显示出高活性的乙二醛酶I。人乙二醛酶I的氨基酸序列在C端三分之二区域与恶臭假单胞菌乙二醛酶I具有57%的同一性，这表明这两种酶可能起源于共同的祖先。
