Monomeric alcohol oxidase is preferentially digested by a novel protease from Candida boidinii

Mary Q. Stewart, Ralf Van Dijk, Marten Veenhuis, Joel M. Goodman

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


A protease activity has been partially purified from peroxisomal matrix fractions of the methylotrophic yeast Candida boidinii. The enzyme migrates as a single peak on a sucrose velocity gradient with an apparent native molecular mass of ∼ 80-90 kDa. Activity can be recovered from nonreducing sodium dodecyl sulfate gels as a ∼ 20 kDa species, suggesting it is an oligomer. The protein exhibits chymotrypsin-like activity and cleaves the model compound suc-L-L-V-Y-AMC. Additionally, monomers of alcohol oxidase (AO), an abundant protein of C. boidinii peroxisomes, generated in vitro or in pulse-radiolabeled cells, are preferentially sensitive to degradation by the protease. Sensitivity is lost over time in vivo as AO folds and matures into octamers, suggesting that the protease may be involved in these processes.

Original languageEnglish (US)
Pages (from-to)160-172
Number of pages13
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number1-3
StatePublished - Jan 30 2002


  • Alcohol oxidase
  • Candida boidinii
  • Microbody
  • Peroxisome
  • Serine protease

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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