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Literature summary for 3.4.24.36 extracted from

  • Pereira, F.M.; Dias, F.A.; Elias, C.G.; dAvila-Levy, C.M.; Silva, C.S.; Santos-Mallet, J.R.; Branquinha, M.H.; Santos, A.L.
    Leishmanolysin-like molecules in Herpetomonas samuelpessoai mediate hydrolysis of protein substrates and interaction with insect (2010), Protist, 161, 589-602.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface surface molecules are glycosylphosphatidylinositol-anchored Herpetomonas pessoai 9986
-
cytoplasm
-
Herpetomonas pessoai 5737
-
extracellular 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 Herpetomonas pessoai
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membrane
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Herpetomonas pessoai 16020
-
additional information 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 Herpetomonas pessoai
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information zinc-metallopeptidase Herpetomonas pessoai

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
x * 66000, SDS-PAGE Herpetomonas pessoai

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Herpetomonas pessoai the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti ?
-
?

Organism

Organism UniProt Comment Textmining
Herpetomonas pessoai
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
promastigote
-
Herpetomonas pessoai
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti Herpetomonas pessoai ?
-
?

Subunits

Subunits Comment Organism
? x * 66000, SDS-PAGE Herpetomonas pessoai

Synonyms

Synonyms Comment Organism
66 kDa surface metallopeptidase
-
Herpetomonas pessoai
leishmanolysin-like molecule
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Herpetomonas pessoai
surface leishmanolysin-like molecule
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Herpetomonas pessoai

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Herpetomonas pessoai

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Herpetomonas pessoai

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
the surface metallopeptidase is active at a broad spectrum of pH Herpetomonas pessoai

General Information

General Information Comment Organism
additional information 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 Herpetomonas pessoai