Study of Umbelliferone Hydroxylation to Esculetin Catalyzed by Polyphenol Oxidase
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- Garcia-Molina Mary of the Sea
- Investigation Group of Enzimology (GENZ), Department of Biochemistry and Molecular Biology A, University of Murcia, Campus of International Excellence “Campus Mare Nostrum”
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- Munoz-Munoz Joseph Louis
- Investigation Group of Enzimology (GENZ), Department of Biochemistry and Molecular Biology A, University of Murcia, Campus of International Excellence “Campus Mare Nostrum”
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- Garcia-Molina Francis
- Investigation Group of Enzimology (GENZ), Department of Biochemistry and Molecular Biology A, University of Murcia, Campus of International Excellence “Campus Mare Nostrum”
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- Rodriguez-Lopez Joseph Neptune
- Investigation Group of Enzimology (GENZ), Department of Biochemistry and Molecular Biology A, University of Murcia, Campus of International Excellence “Campus Mare Nostrum”
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- Garcia-Canovas Francis
- Investigation Group of Enzimology (GENZ), Department of Biochemistry and Molecular Biology A, University of Murcia, Campus of International Excellence “Campus Mare Nostrum”
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Abstract
We characterize umbelliferone, a derivative of 2,4-dihydroxycoumaric acid, as a substrate of polyphenol oxidase. This enzyme hydroxylates umbelliferone to esculetin, its o-diphenol, and then oxidizes it to o-quinone. The findings show that umbelliferone, an intermediate in one of the coumarin biosynthesis pathways, may be transformed into its o-diphenol, esculetin, which is also an intermediate in the same pathway. The activity of the enzyme on umbelliferone was followed by measuring the consumption of oxygen, spectrophotometrically and by HPLC. Kinetic constants characterizing the hydroxylation process were: kcat=0.09±0.02 s−1 and Km=0.17±0.06 mM. The o-diphenol, esculetin, was a better substrate and when its oxidation was followed spectrophotometrically, the kinetic constants were: kcat=1.31±0.25 s−1 and Km=0.035±0.002 mM. Both compounds therefore can be considered as alternative substrates to L-tyrosine and L-3,4-dihydroxyphenylalanine (L-DOPA), since both indirectly inhibit melanogenesis.
Journal
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- Biological and Pharmaceutical Bulletin
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Biological and Pharmaceutical Bulletin 36 (7), 1140-1145, 2013
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679609257472
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- NII Article ID
- 130003361474
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- NII Book ID
- AA10885497
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- COI
- 1:STN:280:DC%2BC3sjmsVKlsg%3D%3D
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- ISSN
- 13475215
- 09186158
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- NDL BIB ID
- 024644662
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- PubMed
- 23811563
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed