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文昌鱼果糖-1,6-二磷酸醛缩酶的分子进化

Molecular evolution of amphioxus fructose-1,6-bisphosphate aldolase.

作者信息

Kuba M, Yatsuki H, Kusakabe T, Takasaki Y, Nikoh N, Miyata T, Yamaguchi T, Hori K

机构信息

Department of Biochemistry, Saga Medical School, Japan.

出版信息

Arch Biochem Biophys. 1997 Dec 15;348(2):329-36. doi: 10.1006/abbi.1997.0384.

Abstract

The cDNA for amphioxus fructose-1,6-bisphosphate (FBP)-aldolase was isolated and its nucleotide sequence was determined. In the cDNA, there existed a probable open reading frame comprising 1080 bp; hence, 359 amino acid residues were deduced. The amino acid sequence indicates the deletion of 4 residues from N-terminus, in comparison with the sequence of FBP-aldolase isozymes from other sources. There was only one FBP-aldolase gene, and one enzyme species corresponding, in the amphioxus; this is the first report of the existence of a single FBP-aldolase species in animals. Enzymatic studies of both native and the recombinant FBP-aldolase suggest that the amphioxus enzyme belongs to an ancestral class I type which is not discovered among vertebrate aldolase isozymes.

摘要

文昌鱼果糖-1,6-二磷酸(FBP)醛缩酶的互补脱氧核糖核酸(cDNA)被分离出来并测定了其核苷酸序列。在该cDNA中,存在一个可能由1080个碱基对组成的开放阅读框;因此,推断出359个氨基酸残基。氨基酸序列表明,与其他来源的FBP醛缩酶同工酶序列相比,文昌鱼FBP醛缩酶的N端缺失了4个残基。文昌鱼中只有一个FBP醛缩酶基因和一种相应的酶;这是关于动物中存在单一FBP醛缩酶种类的首次报道。对天然和重组FBP醛缩酶的酶学研究表明,文昌鱼的这种酶属于一种在脊椎动物醛缩酶同工酶中未发现的原始I类。

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