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Literature summary for 1.1.3.13 extracted from

  • van der Heide, M.; Leao, A.N.; Van der Klei, I.J.; Veenhuis, M.
    Redirection of peroxisomal alcohol oxidase of Hansenula polymorpha to the secretory pathway (2007), FEMS Yeast Res., 7, 1093-1102.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
rerouting of peroxisomal alcohol oxidase to the secretory pathway of Hansenula polymorpha. Using the leader sequence of the Saccharomyces cerevisiae mating factor alpha as sorting signal, alcohol oxidase is correctly sorted to the endoplasmic reticulum. The MFalpha presequence, but not the prosequence, is cleaved from the protein. Alcohol oxidase protein is present in the endoplasmic reticulum as monomers that lack FAD, and hence is enzymatically inactive. The recombinant alcohol oxidase protein is subject to gradual degradation, possibly because the protein does not fold properly. When the Saccharomyces cerevisiae invertase signal sequence is used, secretion of AO protein is observed in conjunction with bulk of the protein being localized to the ER. The amount of secreted AO protein increases with increasing copy numbers of the alcohol oxidase expression cassette integrated into the genome. The secreted alcohol oxidase protein is correctly processed and displays enzyme activity Ogataea angusta

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
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Ogataea angusta 5777
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Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
-
-