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 (Localization
Localization on EC 3.4.24.36 - leishmanolysin
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
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GP63 is able to act on its substrate proteins within the nucleus of its host cell
the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole
additional information
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surface molecules are glycosylphosphatidylinositol-anchored
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about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Surface-localized enzyme is released at different rates from logarithmic and stationary phase virulent promastigotes. Major mechanism regulating enzyme abundance is the rate of loss of surface-localized enzyme from promastigote surface
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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GP63 is able to act on its substrate proteins within the nucleus of its host cell
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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Leishmania mexicana U1103
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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the enzyme is secreted. The zinc-metallopeptidase inhibitor 1,10-phenanthroline is able to restrain the secretion of the metallopeptidase in a dose-dependent manner, while the phospholipase C inhibitor 4-chloromercuriphenylsulfonic acid does not alter the secretion pattern
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promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
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promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
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the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole. The enzyme is released from the parasite surface following phagocytosis and is redistributed to the endoplasmic reticulum of macrophages
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Internal enzyme is stable without detectable decrease in abundance up to 6 days after biosynthesis
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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additional information
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leishmanolysin-like molecules are distributed in different cellular compartments, immunocytochemic analysis, overview. The expression of leishmanolysin-like molecules is not modulated during either temperature- or dimethylsulfoxide-elicited differentiation
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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GP63 is located in punctuated structures along the cell periphery in infected macrophages, with partial colocalization with the lipid raft marker cholera toxin B
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