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Literature summary for 3.4.24.21 extracted from

  • Stepek, G.; McCormack, G.; Birnie, A.J.; Page, A.P.
    The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes (2011), Parasitology, 138, 237-248.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Brugia malayi
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-
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Caenorhabditis elegans
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-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
astacin
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Caenorhabditis elegans
nas-36
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Brugia malayi
nas-36
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Caenorhabditis elegans
nas-36 nas-36 gene encodes a functionally conserved enzyme of the astacin metalloprotease family Brugia malayi
nas-36 nas-36 gene encodes a functionally conserved enzyme of the astacin metalloprotease family Caenorhabditis elegans
nas-37
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Caenorhabditis elegans
nas-37 nas-37 gene encodes a functionally conserved enzyme of the astacin metalloprotease family Caenorhabditis elegans

General Information

General Information Comment Organism
malfunction nas-36 gene from Brugia malayi successfully complements the moult defects associated with Caenorhabditis elegans nas-36, nas-37 and nas-36/nas-37 double mutants Brugia malayi
malfunction the nas-36 and nas-37 genes in Caenorhabditis elegans encode functionally conserved enzymes of the astacin metalloprotease family which, when mutated, result in a phenotype associated with the late-stage moulting defects, namely the inability to remove the preceding cuticle Caenorhabditis elegans