EC Number   |
General Information |
Reference |
|---|
   3.4.24.36 | evolution |
GP63 belongs to the metzincin class, encoded by a series of tandemly linked genes usually in a single chromosome that are highly sequence-conserved among different species of Leishmania |
-, 717290 |
| 3.4.24.36 | malfunction |
a leishmanolysin knockout strain of Leishmania major Seidman strain lacks the GP63 surface metalloprotease |
-, 718253 |
| 3.4.24.36 | more |
Herpetomonas samuelpessoai cells are able to colonize the gut of Aedes aegypti, but the pretreatment of gut cells with purified leishmanolysin-like protein drastically diminishes the adhesion, overview. The expression of surface leishmanolysin in Herpetomonas samuelpessoai cells is drastically enhanced after passage in Aedes aegypti |
710519 |
| 3.4.24.36 | more |
homology modeling and structure-function relationship of GP63, overview |
-, 717290 |
| 3.4.24.36 | more |
the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview |
-, 718253 |
| 3.4.24.36 | physiological function |
GP63 is a key Leishmania virulence factor. Leishmania GP63 alters the profile of protein tyrosine phosphatases associated with JAK-2 at the host cell plasma membrane |
710559 |
| 3.4.24.36 | physiological function |
Leishmania-induced inactivation of the macrophage transcription factor AP-1 is mediated by the parasite metalloprotease GP63 at the cell surface, overview. GP63 but not LPG is highly involved in the mechanism responsible for the inactivation of AP-1 transcription factor. GP63 action requires macrophage lipid raft and is not dependent on parasite phagocytosis |
718304 |
| 3.4.24.36 | physiological function |
metalloprotease GP63 is the major Leishmania surface antigen. It has multiple functions required for the survival of the parasite. Metalloprotease GP63 is encoded by multiple genes and their copy numbers vary considerably between different species. A greater role for the sequence variation found among the chromosome 10 GP63 genes is possibly related to the pathogenesis of Leishmania braziliensis and closely related species within the mammalian host |
753098 |
| 3.4.24.36 | physiological function |
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the host's immune functions, allowing the survival of the parasite and its dissemination |
754989 |
| 3.4.24.36 | physiological function |
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination |
754989 |
