Summary
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1.
The substrate specificity of three different molecular forms of laccase has been determined with a polarographic method using 31 phenolic compounds and ascorbic acid.
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2.
Whereas the two low molecular weight laccases II and III are in general able to oxidize phenolic compounds containing at least two hydroxy (or amino-)groups independent of their position on the aromatic ring; the high molecular weight laccase I is only able to catalyze the oxidation of p- and o-diphenols and does not attack m-phenols (with the exception of phloroglucinol). Ascorbic acid is oxidized by all three molecular species.
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3.
After freezing and thawing several times, the catalytic ability of laccase I is extended to the oxidation of some m-phenols.
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4.
A possible correlation between the conformation of the laccase molecule and its capacity to oxidize m-phenols is discussed.
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5.
It is proposed to alter in the official “enzyme nomenclature” the definition of laccase to: Diphenol: oxygen oxidoreductase, with the restriction that the affinity for m-phenols depends on a special molecular structure of the enzyme.
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With support of the Deutsche Forschungsgemeinschaft, Bad Godesberg, and of the Landesamt für Forschung, Düsseldorf.
Supported by a fellowship of the Humboldt-Stiftung, Bad Godesberg.
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Scháněl, L., Esser, K. The phenoloxidases of the Ascomycete Podospora anserina . Archiv. Mikrobiol. 77, 111–117 (1971). https://doi.org/10.1007/BF00408603
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DOI: https://doi.org/10.1007/BF00408603