Characterization of ascorbate oxidase from Acremonium sp. HI-25.

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 Biochem

journal_title

Journal of biochemistry

authors

Hirose J,Sakurai T,Imamura K,Watanabe H,Iwamoto H,Hiromi K,Itoh H,Shin T,Murao S

doi

10.1093/oxfordjournals.jbchem.a124420

subject

Has Abstract

pub_date

1994-05-01 00:00:00

pages

811-3

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

115

pub_type

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