果糖-1,6-二磷酸酶。兔肝酶的一级结构。寡聚蛋白的“中等程度”变异性。

Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver enzyme. 'Intermediate' variability of an oligomeric protein.

作者信息

Kaiser R, Olsson H, Erman M, Weeks C M, Hjelmqvist L, Ghosh D, Jörnvall H

机构信息

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.

出版信息

FEBS Lett. 1996 Jul 8;389(3):249-52. doi: 10.1016/0014-5793(96)00594-7.

DOI:10.1016/0014-5793(96)00594-7

PMID:8766709

Abstract

The primary structure of rabbit liver fructose-1,6-bisphosphatase was determined by peptide analysis of digests with different proteases. The results establish the primary structure, complete data bank entries, and show that this enzyme variant is indeed homologous with other liver fructose-1,6-bisphosphatases. Residue differences with the enzymes from other mammals are 9-15%, with those from plants and yeasts about 50%, and with those from characterized prokaryotes up to 70%, showing an enzyme variability intermediate between those of 'variable' and 'constant' oligomeric dehydrogenases. Structural relationships, conformations and catalytic mechanisms are consistent within the family of fructose-1,6-bisphosphatases, and the rabbit protein is a typical rather than an aberrant form of the enzyme.

摘要

通过对不同蛋白酶消化产物进行肽分析，确定了兔肝果糖-1,6-二磷酸酶的一级结构。结果确定了一级结构，完善了数据库条目，并表明这种酶变体确实与其他肝果糖-1,6-二磷酸酶同源。与其他哺乳动物的酶相比，残基差异为9%-15%，与植物和酵母的酶相比约为50%，与已鉴定的原核生物的酶相比高达70%，表明该酶的变异性处于“可变”和“恒定”寡聚脱氢酶之间。在果糖-1,6-二磷酸酶家族中，结构关系、构象和催化机制是一致的，兔蛋白是该酶的典型形式而非异常形式。