Abstract
Autocatalytic formation of His-Cys cross-linkage in the enzyme active site of tyrosinase from Aspergillus oryzae has been demonstrated to proceed by the treatment of apoenzyme with Cu(II) under aerobic conditions, where a (μ-η(2):η(2)-peroxo)dicopper(II) species has been suggested to be involved as a key reactive intermediate.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aspergillus oryzae / enzymology
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Biocatalysis
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Copper / chemistry*
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Cross-Linking Reagents / chemistry
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Cross-Linking Reagents / pharmacology
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Cysteine / chemistry*
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Histidine / chemistry*
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Models, Molecular
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Monophenol Monooxygenase / chemistry*
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Monophenol Monooxygenase / metabolism*
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Organometallic Compounds / chemistry
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Organometallic Compounds / pharmacology*
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Protein Conformation
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Protein Processing, Post-Translational / drug effects*
Substances
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Cross-Linking Reagents
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Organometallic Compounds
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Histidine
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Copper
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Monophenol Monooxygenase
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Cysteine