Monomeric alcohol oxidase is preferentially digested by a novel protease from Candida boidiniiStewart, M. Q., Dijk, R. V., Veenhuis, M. & Goodman, J. M., 30-Jan-2002, In : Biochimica et Biophysica Acta-Molecular Cell Research. 1542, 1-3, p. 160-172 13 p., PII S0167-4889(01)00176-8.
Research output: Contribution to journal › Article › Academic
A protease activity has been partially purified from peroxisomal matrix fractions of the methylotrophic yeast Candida hoidinii. The enzyme migrates as a single peak on a sucrose velocity gradient with an apparent native molecular mass of similar to 80-90 kDa. Activity can be recovered from nonreducing sodium dodecyl sulfate gels as a similar to 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. (C) 2002 Elsevier Science B.V. All rights reserved.
|Article number||PII S0167-4889(01)00176-8|
|Number of pages||13|
|Journal||Biochimica et Biophysica Acta-Molecular Cell Research|
|Publication status||Published - 30-Jan-2002|
- peroxisome: microbody, serine protease, alcohol oxidase, Candida boidinii, HANSENULA-POLYMORPHA, MEMBRANE-PROTEINS, IMPORT, PEROXISOMES, THIOLASE, METHANOL, ENZYME, STEP