Kawamoto S, Amaya Y, Murakami K, Tokunaga F, Iwanaga S, Kobayashi K, Saheki T, Kimura S, Mori M
J Biol Chem. 1987 May 5;262(13):6280-3.
Arginase (EC 3.5.3.1) catalyzes the last step of urea synthesis in the liver of ureotelic animals. The nucleotide sequence of rat liver arginase cDNA, which was isolated previously (Kawamoto, S., Amaya, Y., Oda, T., Kuzumi, T., Saheki, T., Kimura, S., and Mori, M. (1986) Biochem. Biophys. Res. Commun. 136, 955-961) was determined. An open reading frame was identified and was found to encode a polypeptide of 323 amino acid residues with a predicted molecular weight of 34,925. The cDNA included 26 base pairs of 5'-untranslated sequence and 403 base pairs of 3'-untranslated sequence, including 12 base pairs of poly(A) tract. The NH2-terminal amino acid sequence, and the sequences of two internal peptide fragments, determined by amino acid sequencing, were identical to the sequences predicted from the cDNA. Comparison of the deduced amino acid sequence of the rat liver arginase with that of the yeast enzyme revealed a 40% homology.
精氨酸酶（EC 3.5.3.1）催化排尿素动物肝脏中尿素合成的最后一步。此前已分离出大鼠肝脏精氨酸酶cDNA（河本，S.，天谷，Y.，小田，T.，久住，T.，佐伯，T.，木村，S.，和森，M.（1986年）《生物化学与生物物理学研究通讯》136，955 - 961），并测定了其核苷酸序列。确定了一个开放阅读框，发现它编码一个由323个氨基酸残基组成的多肽，预测分子量为34,925。该cDNA包含26个碱基对的5' - 非翻译序列和403个碱基对的3' - 非翻译序列，包括12个碱基对的聚腺苷酸尾。通过氨基酸测序确定的NH2 - 末端氨基酸序列以及两个内部肽段的序列与从cDNA预测的序列相同。大鼠肝脏精氨酸酶推导的氨基酸序列与酵母酶的氨基酸序列比较显示出40%的同源性。
