1. Molecular cloning of capillary permeability-increasing enzyme-2 from Agkistrodon caliginosus (Korean viper)
- Author
-
Bum-Soo Hahn, Il-Moo Chang, Yeong Shik Kim, Wan-Seok Kim, Chang-Soo Lee, and Kwanghee Baek
- Subjects
Signal peptide ,DNA, Complementary ,Molecular Sequence Data ,Viper Venoms ,Biology ,Toxicology ,Zymogen ,Complementary DNA ,Animals ,Amino Acid Sequence ,Cloning, Molecular ,Peptide sequence ,Gene Library ,chemistry.chemical_classification ,Serine protease ,Base Sequence ,cDNA library ,Serine Endopeptidases ,Nucleic acid sequence ,Blotting, Northern ,Molecular biology ,Enzymes ,Amino acid ,Biochemistry ,chemistry ,biology.protein ,Agkistrodon - Abstract
The gene of capillary permeability-increasing enzyme-2 (CPI enzyme-2) was cloned from the cDNA library of Agkistrodon caliginosus and its nucleotide sequence was determined. Its sequence indicates that CPI enzyme-2 is synthesized as a pre-zymogen of 258 amino acid residues, including a putative secretory signal peptide of 18 amino acids and a proposed zymogen peptide of 6 amino acids. The amino terminal sequence deduced from the cDNA sequence was exactly consistent with that of CPI enzyme-2 except for the substitution of an amino acid (Gly27--Ser). The open reading frame is very similar to those of plasminogen activator and thrombin-like proteases cloned from other snakes. The clone encoding CPI enzyme-2 belongs to the serine protease family. The active site of the enzyme is highly conserved at His41, Asp86 and Ser180. Its possible glycosylation sites, Asn-X-Thr/Ser, are located at amino acid residues 20-22, 55-57, 79-81 and 97-99.
- Published
- 1998