The amino-acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function.
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.
Syntichaki
K M
KM
Department of Biology, University of Crete, Heraklion, Greece.
Loulakakis
K A
KA
Roubelakis-Angelakis
K A
KA
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D004795:Enzyme Stability / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D005638:Fruit / Q000201:enzymology* / Q000235:genetics; D017343:Genes, Plant; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000235:genetics; D005974:Glutamate-Ammonia Ligase / Q000235:genetics; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010802:Phylogeny; D010944:Plants / Q000201:enzymology / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017421:Sequence Analysis; D012689:Sequence Homology, Nucleic Acid
D011993:Recombinant Fusion Proteins; D005969:Glutamate Dehydrogenase; D005974:Glutamate-Ammonia Ligase