3.4.24.36: leishmanolysin
This is an abbreviated version!
For detailed information about leishmanolysin, go to the full flat file.
Word Map on EC 3.4.24.36
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3.4.24.36
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promastigotes
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pneumocystis
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leishmaniasis
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carinii
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donovani
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trypanosoma
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amastigotes
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jirovecii
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mexicana
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chaga
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pcp
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guanidinobenzoatase
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infantum
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lipophosphoglycan
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metacyclic
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braziliensis
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complement-mediated
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phagolysosome
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amazonensis
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rat-derived
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9-amino
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tsetse
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viannia
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leishmanial
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medicine
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procyclins
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pharmacology
- 3.4.24.36
- promastigotes
- pneumocystis
- leishmaniasis
- carinii
- donovani
- trypanosoma
- amastigotes
- jirovecii
- mexicana
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chaga
- pcp
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guanidinobenzoatase
- infantum
- lipophosphoglycan
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metacyclic
- braziliensis
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complement-mediated
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phagolysosome
- amazonensis
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rat-derived
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9-amino
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tsetse
- viannia
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leishmanial
- medicine
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procyclins
- pharmacology
Reaction
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-/-Leu-Lys-Lys- =
Synonyms
66 kDa surface metallopeptidase, Cell surface protease, glycoprotein 63, Glycoprotein gp63, gp63, GP63 metalloprotease, GP63 protein, GP63 surface metalloprotease, GP63 virulence protein, Leishmania metalloproteinase, Leishmania surface metalloprotease, leishmanolysin-like molecule, Major surface glycoprotein, major surface protease, major surface-metalloprotease, metalloprotease GP63, MSP, Promastigote surface endopeptidase, Promastigote surface protease, protective surface protease, Surface acid proteinase, surface leishmanolysin-like molecule, surface protease GP63, surface protein GP63, surface proteinase GP63, virulence factor major surface protease
ECTree
3.4.24.36 leishmanolysinAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.36 - leishmanolysin
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protein tyrosine phosphatase PTP1B + H2O
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activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
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protein tyrosine phosphatase SHP-1 + H2O
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activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
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protein tyrosine phosphatase TCPTP + H2O
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activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
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additional information
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the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti
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additional information
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protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
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additional information
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protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
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additional information
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major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
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additional information
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major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
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additional information
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role of enzyme in promastigote multiplication connected with its fibronectin-like properties
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additional information
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Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
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additional information
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enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
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additional information
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the major surface-metalloprotease is a virulence factor which contributes to a variety of functions including evasion of complement-mediated parasite-killing and host intramacrophage survival, the protozoan enzyme protects the parasite against antimicrobial peptide-induced apoptotic killing by the host cell, overview
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additional information
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gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
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additional information
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gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
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additional information
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gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania
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additional information
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Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
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additional information
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Leishmania mexicana pifanoi
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protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
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