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5′-Nucleotidase from the electric ray electric lobe.
- Source :
- European Journal of Biochemistry; 12/18/91, Vol. 202 Issue 3, p855-861, 7p
- Publication Year :
- 1991
-
Abstract
- A cDNA encoding a 5′-nucleotidase was identified by screening a λgt10 cDNA library from the electric lobe of Discopyge ommata using a cDNA probe containing the complete open reading frame coding for the rat liver enzyme. Nucleotide sequence analysis defines an open reading frame of 577 amino acids, corresponding to a calculated molecular mass of 63833 Da. The N-terminus of the mature protein, as determined by direct protein sequencing, is preceded by 29 amino acid residues comprising a signal peptide. The C-terminus contains a stretch of hydrophobic amino adds, considered to be cleaved on post-translational modification and exchanged for glycosylphosphatidylinositol as a membrane anchor. The predicted protein contains four potential N-linked glycosylation sites. Electric ray 5′-nucleotidase shares 61 % amino acid identity with the enzymes from rat liver and human placenta, and about 23% with bacterial proteins possessing 5′-nucleotidase activity and also additional enzyme activities like UDP-glucose hydrolase. Polyclonal antibodies raised against 5′-nucleotidase from mammalian sources or the electric ray electric organ reveal mutual cross-reactivity. Interestingly, there are 5–7 domains highly conserved in procaryotes and vertebrates in enzymes exhibiting 5′-nucleotidase, 3′-nucleotidase or phosphodiesterase activity. 5′-nucleotidase isolated from Torpedo electric organ hydrolyzes UDP-glucose at 8% of the rate of AMP hydrolysis. The possible phylogenetic origin of vertebrate 5′-nucleotidase from multifunctional nucleotide hydrolases is discussed. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 202
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15826598
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1991.tb16443.x