Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)

• Published in: The Journal of biological chemistry 1988-03, Vol.263 (8), p.3550-3553
• Main Authors: Merlie, J P, Fagan, D, Mudd, J, Needleman, P
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA - genetics; DNA - isolation & purification; DNA Restriction Enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Genes; Male; Molecular Sequence Data; Oxidoreductases; Prostaglandin-Endoperoxide Synthases - genetics; Protein Conformation; Seminal Vesicles - enzymology; Sheep
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)68959-8

An oligonucleotide probe was used to isolate a clone encoding prostaglandin endoperoxide synthetase (cyclooxygenase, EC 1.14.99.1) from a sheep seminal vesicle cDNA library. The protein predicted from nucleic acid sequence contains 599 amino acids including a 23-amino acid signal sequence. Thus, the mature cyclooxygenase deduced from the cDNA compares favorably in molecular size to the 70-kDa protein determined by gel electrophoresis. A putative transmembrane region and potential carbohydrate addition sites for N-linked sugars can be inferred from the amino acid sequence. Significantly, sequence similarities exist between cyclooxygenase, myeloperoxidase, and several other heme-containing proteins. The putative glycosylation sites, transmembrane domain, and sequence similarities with functionally related enzymes have been incorporated into a model for the topology of cyclooxygenase in the endoplasmic reticulum.