The active site of galactose oxidase.
نویسندگان
چکیده
منابع مشابه
The 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...
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The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. A structure of this protein has previously been proposed based on an assumed structural homology to the di-iron carboxylate family of proteins. However, these authors suggested the protein has a very different topology than the known structures of di-iron carboxyla...
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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...
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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...
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Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)68751-4