The amino-acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function

被引：40

作者：

Syntichaki, KM ^{[1
]}

Loulakakis, KA ^{[1
]}

RoubelakisAngelakis, KA ^{[1
]}

机构：

[1] UNIV CRETE,DEPT BIOL,GR-71110 CRETE,GREECE

来源：

GENE | 1996年 / 168卷 / 01期

关键词：

Vitis vinifera; cDNA; nitrogen metabolism; sequence;

D O I：

10.1016/0378-1119(96)83097-6

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

A cDNA clone encoding grapevine (Vitis vinifera L. cv Sultanina) NAD(H)-glutamate dehydrogenase (GDH) was isolated from a cDNA expression library by immunoscreening with a polyclonal antibody raised against grapevine GDH. Nucleotide sequence analysis revealed an open reading frame (ORF) encoding a precursor protein of 411 amino acids (aa) with a calculated molecular mass of 44.517 kDa. The deduced aa sequence showed relatively higher homology to GDH from archaebacteria species, than to those from eukaryotes and eubacteria. This resemblance indicated a functional and/or evolutionary relationship in this class of enzymes which might be relevant to the stress-related function of plant GDH, We have shown that the bacterially produced plant GDH was thermostable.

引用

页码：87 / 92

页数：6

共 24 条

[1] SUBUNIT ASSEMBLY AND ACTIVE-SITE LOCATION IN THE STRUCTURE OF GLUTAMATE-DEHYDROGENASE [J].