Abstract
This chapter discusses the activity, specificity and structural chemistry of jararhagin. Jararhagin is a single-chain hemorrhagic endopeptidase with a molecular mass of approximately 52 kDa and a pi of 4.5. The enzyme is a class III reprolysin comprising a metalloprotease domain and a C-terminal disintegrin domain. A propeptide sequence is predicted in the cDNA, indicating that the enzyme is synthesized as an inactive zymogen. In the disintegrin domain the Arg-Gly-Asp sequence is replaced by Glu-Cys-Asp. A high degree of overall sequence similarity exists with other members of the reprolysin family. Preliminary diffraction data to a resolution of 2.8 Å has been obtained from crystallized jararhagin. The natural function of venom is to immobilize and kill prey. The broad substrate specificity and hemorrhagic nature of jararhagin indicates that it probably contributes substantially to the lethal activity of B. jararaca venom and may play a role in prey digestion. Jararhagin is considered to be one of the major components responsible for local and systemic hemorrhage following envenomation by Brazilian pit viper, B. jararaca.
| Original language | English |
|---|---|
| Title of host publication | Handbook of Proteolytic Enzymes, Second Edition: Volume 1: Aspartic and Metallo Peptidases |
| Pages | 654-656 |
| Number of pages | 3 |
| Volume | 1 |
| ISBN (Electronic) | 9780120796113 |
| DOIs | |
| Publication status | Published - 1 Jan 2004 |
| Externally published | Yes |