The d-Galactose Oxidase of Polyporus circinatus
نویسندگان
چکیده
منابع مشابه
The D-galactose oxidase of Polyporus circinatus.
The mold Polyporus circinatus produces an extracellular oxidase that catalyzes the oxidation of n-galactose (1). The reaction appears superficially to be similar to the oxidation of n-glucose catalyzed by notatin (2)) and can be followed by measuring the consumption of oxygen or the production of Hz02 (1). The enzyme is useful for the determination of galactose, employing the same peroxidase-ch...
متن کاملGalactose oxidase of Polyporus circinatus: a copper enzyme.
In 1959, Cooper et al. (1) described the isolation of an enzyme from Polyporus circinatus Fr. which catalyzed the oxidation of galactose by molecular oxygen. MTe have previously described a procedure for the purification of such an enzyme from culture filtrat,es and have shown the reaction product to be D-g&CtOhexodialdose, oxidation occurring at the C-6 rather than the C-l position (2). The pr...
متن کاملThe Estimation of Galactose in Plasma Using Galactose Oxidase.
The estimation of galactose in plasma by the enzyme system galactose oxidaseperoxidase was investigated. The method was found to be relatively specific for galactose although xylose and ascorbic acid reacted to a slight degree with the enzyme; lactose also reacted with the enzyme, probably because partial hydrolysis of the disaccharide released galactose. The relationship between absorbance and...
متن کاملThe radical chemistry of galactose oxidase.
Galactose oxidase is a free radical metalloenzyme containing a novel metalloradical complex, comprised of a protein radical coordinated to a copper ion in the active site. The unusually stable protein radical is formed from the redox-active side chain of a cross-linked tyrosine residue (Tyr-Cys). Biochemical studies on galactose oxidase have revealed a new class of oxidation mechanisms based on...
متن کاملCofactor processing in galactose oxidase.
GO (galactose oxidase; E.C. 1.1.3.9) is a monomeric 68 kDa enzyme that contains a single copper ion and an amino acid-derived cofactor. The enzyme is produced by the filamentous fungus Fusarium graminearum as an extracellular enzyme. The enzyme has been extensively studied by structural, spectroscopic, kinetic and mutational approaches that have provided insight into the catalytic mechanism of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1962
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)60220-0