Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.21 extracted from

  • Baska, P.; Wisniewski, M.; Krzyzowska, M.; Dlugosz, E.; Zygner, W.; Gorski, P.; Wedrychowicz, H.
    Molecular cloning and characterisation of in vitro immune response against astacin-like metalloprotease Ace-MTP-2 from Ancylostoma ceylanicum (2013), Exp. Parasitol., 133, 472-482.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene Ace-mtp-2, DNA and amino acid seuence determination and analysis, recombinant expression in Escherichia coli strains BL21 and Rosetta and Pichia pastoris strain X33 Ancylostoma ceylanicum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the protease has a putative signal peptide and is secreted Ancylostoma ceylanicum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc metalloprotease Ancylostoma ceylanicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26700
-
x * 26700, about, sequence calculation Ancylostoma ceylanicum

Organism

Organism UniProt Comment Textmining
Ancylostoma ceylanicum Q0Z889 gene Ace-mtp-2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis Ancylostoma ceylanicum

Source Tissue

Source Tissue Comment Organism Textmining
additional information highest enzyme expression level occurs in the adult stage of the parasite Ancylostoma ceylanicum
-

Subunits

Subunits Comment Organism
? x * 26700, about, sequence calculation Ancylostoma ceylanicum

Synonyms

Synonyms Comment Organism
Ace-MTP-2
-
Ancylostoma ceylanicum
Ancylostoma ceylanicum metalloprotease 2
-
Ancylostoma ceylanicum
astacin-like metalloprotease
-
Ancylostoma ceylanicum

General Information

General Information Comment Organism
additional information the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis Ancylostoma ceylanicum
physiological function the protease is working at the host–parasite interface and is likely be exposed to the hosts immune response. Recombinant Ace-MTP-2 amplifies the in vitro release of TNFalpha and induces release of IFNgamma by lipopolysaccharide activated THP-1 macrophages, overview Ancylostoma ceylanicum