Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog.
Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog.
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牛肺前列腺素 F 合酶与欧洲青蛙晶状体ε-晶状体蛋白的结构相似性。
DOI：
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发表时间：
1988
影响因子：
11.1
通讯作者：
O. Hayaishi
中科院分区：
文献类型：
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作者：
Kikuko Watanabe;Y. Fujii;Kazuhisa Nakayama;H. Ohkubo;S. Kuramitsu;H. Kagamiyama;S. Nakanishi;O. Hayaishi
从牛肺基因文库中克隆了前列腺素F(PGF)合成酶特异的cDNA序列。核苷酸序列分析表明，PGF合成酶由一个969碱基的开放阅读框组成，编码一个由323个氨基酸组成的多肽，Mr为36,666。序列分析表明，与人肝醛还原酶[Wermuth，B.，Omar，A.，Forster，A.，Francesco，C.，Wolf，M.，Wartburg，J.P.，Bullock，B.&Gabbay，K.H.(1987)]相比，牛肺PGF合成酶有62%的同源性和保守性替换。Weiner，H.&Flynn，T.G.(Liss，New York)，pp.297-307]它在相对分子质量和底物专一性上与PGF合成酶相似。然而，PGF合成酶的氨基酸序列与国家生物医学研究基金会蛋白质数据库的比较表明，来自欧洲普通蛙(Rana Temporaria)[Tomarev，S.I.，Zinovieva，R.D.，Dolgilevich，S.M.，Luchin，S.V.，Krayev，A.S.，Skryabin，K.G.&Guss，G.G.(1984)FEBS Lett]的PGF合成酶C末端的225个氨基酸序列。171,297-302]和PGF合成酶的序列显示77%的相同和保守的替换，没有缺失/增加。这一结果表明，欧洲普通蛙晶状体中的epsilon-crystallin与牛肺PGF合成酶是一致的。
Cloned cDNA sequences specific for prostaglandin F (PGF) synthase have been isolated from a cDNA library of bovine lung mRNA sequences. Nucleotide-sequence analyses of cloned cDNA inserts have revealed that PGF synthase consists of a 969-base pair open reading frame coding for a 323-amino acid polypeptide with a Mr of 36,666. The sequence analysis indicates that bovine lung PGF synthase shows 62% identical plus conservative substitutions compared with human liver aldehyde reductase [Wermuth, B., Omar, A., Forster, A., Francesco, C., Wolf, M., Wartburg, J.P., Bullock, B. & Gabbay, K.H. (1987) in Enzymology and Molecular Biology of Carbonyl Metabolism: Aldehyde Dehydrogenase, Aldo-Keto Reductase, and Alcohol Dehydrogenase, eds. Weiner, H. & Flynn, T.G. (Liss, New York), pp. 297-307], which is similar to PGF synthase in molecular weight and substrate specificity. However, comparison of the amino acid sequence of PGF synthase with the National Biomedical Research Foundation protein data base reveals that the sequences of 225 amino acids from C termini of epsilon-crystallin of the European common frog (Rana temporaria) [Tomarev, S.I., Zinovieva, R.D., Dolgilevich, S.M., Luchin, S.V., Krayev, A.S., Skryabin, K.G. & Gause, G.G. (1984) FEBS Lett. 171, 297-302] and of PGF synthase show 77% identical and conservative substitutions without deletions/additions. The result suggests that European common frog lens epsilon-crystallin is identical to bovine lung PGF synthase.