Abstract:
:Alcohol oxidase (AO) is a peroxisomal, homo-octameric flavoenzyme, which catalyzes methanol oxidation in methylotrophic yeast. Here, we report on the generation of soluble, FAD-lacking AO monomers. Using steady-state fluorescence, fluorescence correlation spectroscopy, circular dichroism and static light scattering approaches, we demonstrate that FAD-lacking AO monomers are formed upon incubation of purified, native octameric AO in a solution containing 50% dimethylsulfoxide (DMSO). Upon removal of DMSO the protein remained monomeric and soluble and did not contain FAD. Binding experiments revealed that the AO monomers bind to purified pyruvate carboxylase, a protein that plays a role in the formation of enzymatically active AO octamers in vivo.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Visser NV,Wang D,Stanley WA,Groves MR,Wilmanns M,Veenhuis M,van der Klei IJdoi
10.1016/j.abb.2007.01.005subject
Has Abstractpub_date
2007-03-15 00:00:00pages
208-13issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(07)00012-4journal_volume
459pub_type
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