Abstract:
:The ascorbate oxidase obtained from a microorganism, Acremonium sp. HI-25 (molecular weight, 80 kDa; monomeric protein), was studied with respect to atomic absorption, EPR, absorption spectra, circular dichroism (CD) spectra, and steady-state kinetics. The enzyme was found to be a multicopper protein, containing four copper atoms of three kinds, types 1, 2, and 3 copper, in the ratio of 1:1:2. The EPR parameters of the type 1 and 2 copper atoms in the ascorbate oxidase are very similar to those in the case of the ascorbate oxidase obtained from cucumber, which is a dimeric protein. The apparent Km and kcat values for ascorbic acid of the ascorbate oxidase from Acremonium sp. HI-25 are almost the same as those of the monomeric unit of the ascorbate oxidase from cucumber.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Hirose J,Sakurai T,Imamura K,Watanabe H,Iwamoto H,Hiromi K,Itoh H,Shin T,Murao Sdoi
10.1093/oxfordjournals.jbchem.a124420subject
Has Abstractpub_date
1994-05-01 00:00:00pages
811-3issue
5eissn
0021-924Xissn
1756-2651journal_volume
115pub_type
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