Kinetics of Mushroom Tyrosinase Inhibition by Quercetin
The effects of quercetin on the activity of mushroom tyrosinase were studied. The equilibrium constants for this inhibitor binding with the enzyme molecule were established. The inhibition mechanism obtained from Lineweaver−Burk plots show that quercetin is a competitive inhibitor. In the time cours...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2002-07, Vol.50 (14), p.4108-4112 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Chen, Qing-Xi Kubo, Isao |
| description | The effects of quercetin on the activity of mushroom tyrosinase were studied. The equilibrium constants for this inhibitor binding with the enzyme molecule were established. The inhibition mechanism obtained from Lineweaver−Burk plots show that quercetin is a competitive inhibitor. In the time course of the oxidation of l-3,4-dihydroxyphenylalanine (l-DOPA) catalyzed by the enzyme in the presence of different concentrations of quercetin, the rate decreased with increasing time until a straight line was approached. The inhibition of tyrosinase by quercetin is a slow and reversible reaction with residual enzyme activity. The microscopic rate constants were determined for the reaction of quercetin with the enzyme. Keywords: Tyrosinase inhibitory activity; quercetin; kinetics; competitive inhibition |
| doi_str_mv | 10.1021/jf011378z |
| format | Article |
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The equilibrium constants for this inhibitor binding with the enzyme molecule were established. The inhibition mechanism obtained from Lineweaver−Burk plots show that quercetin is a competitive inhibitor. In the time course of the oxidation of l-3,4-dihydroxyphenylalanine (l-DOPA) catalyzed by the enzyme in the presence of different concentrations of quercetin, the rate decreased with increasing time until a straight line was approached. The inhibition of tyrosinase by quercetin is a slow and reversible reaction with residual enzyme activity. The microscopic rate constants were determined for the reaction of quercetin with the enzyme. 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Agric. Food Chem</addtitle><description>The effects of quercetin on the activity of mushroom tyrosinase were studied. The equilibrium constants for this inhibitor binding with the enzyme molecule were established. The inhibition mechanism obtained from Lineweaver−Burk plots show that quercetin is a competitive inhibitor. In the time course of the oxidation of l-3,4-dihydroxyphenylalanine (l-DOPA) catalyzed by the enzyme in the presence of different concentrations of quercetin, the rate decreased with increasing time until a straight line was approached. The inhibition of tyrosinase by quercetin is a slow and reversible reaction with residual enzyme activity. The microscopic rate constants were determined for the reaction of quercetin with the enzyme. Keywords: Tyrosinase inhibitory activity; quercetin; kinetics; competitive inhibition</description><subject>Agaricales - enzymology</subject><subject>Agronomy. Soil science and plant productions</subject><subject>Biological and medical sciences</subject><subject>Economic plant physiology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Kinetics</subject><subject>Levodopa - metabolism</subject><subject>Medical sciences</subject><subject>Metabolism</subject><subject>Monophenol Monooxygenase - antagonists & inhibitors</subject><subject>Monophenol Monooxygenase - metabolism</subject><subject>Nutrition. Photosynthesis. Respiration. Metabolism</subject><subject>Oxidation-Reduction</subject><subject>Pharmacognosy. Homeopathy. Health food</subject><subject>Pharmacology. Drug treatments</subject><subject>Plant physiology and development</subject><subject>Quercetin - pharmacology</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0E1Lw0AQBuBFFFurB_-A5KLgIbqfyfao1WqxfmHuy2YzoVubpO4mYP31rrS0F0_DMA8vw4vQKcFXBFNyPS8xISyVP3uoTwTFsSBE7qM-DsdYioT00JH3c4yxFCk-RD1CsWRySPsofbI1tNb4qCmj587PXNNUUbZyjbe19hBN6pnNbWubOspX0XsHzgRfH6ODUi88nGzmAGXj-2z0GE9fHyajm2msORdtXFIDjIuCMpNgTTQUhkrIIc95QUtBeJJTDJIYEIJzKqgkQgzDUsAw55gN0MU6dumarw58qyrrDSwWuoam8yolUmCRiAAv19CEz72DUi2drbRbKYLVX0lqW1KwZ5vQLq-g2MlNKwGcb4D2Ri9Kp2tj_c6xNGEskcHFa2d9C9_bu3afKklZKlT29qHkC-UyG9-qu12uNl7Nm87Vobp_HvwFZn-JDQ</recordid><startdate>20020703</startdate><enddate>20020703</enddate><creator>Chen, Qing-Xi</creator><creator>Kubo, Isao</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020703</creationdate><title>Kinetics of Mushroom Tyrosinase Inhibition by Quercetin</title><author>Chen, Qing-Xi ; Kubo, Isao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-f2ce345d23c60a1aedc28ebebb4d2f5146b20e81ce554425281559e55de9b403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Agaricales - enzymology</topic><topic>Agronomy. Soil science and plant productions</topic><topic>Biological and medical sciences</topic><topic>Economic plant physiology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Kinetics</topic><topic>Levodopa - metabolism</topic><topic>Medical sciences</topic><topic>Metabolism</topic><topic>Monophenol Monooxygenase - antagonists & inhibitors</topic><topic>Monophenol Monooxygenase - metabolism</topic><topic>Nutrition. Photosynthesis. Respiration. Metabolism</topic><topic>Oxidation-Reduction</topic><topic>Pharmacognosy. Homeopathy. Health food</topic><topic>Pharmacology. Drug treatments</topic><topic>Plant physiology and development</topic><topic>Quercetin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Qing-Xi</creatorcontrib><creatorcontrib>Kubo, Isao</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Qing-Xi</au><au>Kubo, Isao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of Mushroom Tyrosinase Inhibition by Quercetin</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-07-03</date><risdate>2002</risdate><volume>50</volume><issue>14</issue><spage>4108</spage><epage>4112</epage><pages>4108-4112</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The effects of quercetin on the activity of mushroom tyrosinase were studied. The equilibrium constants for this inhibitor binding with the enzyme molecule were established. The inhibition mechanism obtained from Lineweaver−Burk plots show that quercetin is a competitive inhibitor. In the time course of the oxidation of l-3,4-dihydroxyphenylalanine (l-DOPA) catalyzed by the enzyme in the presence of different concentrations of quercetin, the rate decreased with increasing time until a straight line was approached. The inhibition of tyrosinase by quercetin is a slow and reversible reaction with residual enzyme activity. The microscopic rate constants were determined for the reaction of quercetin with the enzyme. Keywords: Tyrosinase inhibitory activity; quercetin; kinetics; competitive inhibition</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12083892</pmid><doi>10.1021/jf011378z</doi><tpages>5</tpages></addata></record> |
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| subjects | Agaricales - enzymology Agronomy. Soil science and plant productions Biological and medical sciences Economic plant physiology Enzyme Inhibitors - pharmacology Enzymes Fundamental and applied biological sciences. Psychology General pharmacology Kinetics Levodopa - metabolism Medical sciences Metabolism Monophenol Monooxygenase - antagonists & inhibitors Monophenol Monooxygenase - metabolism Nutrition. Photosynthesis. Respiration. Metabolism Oxidation-Reduction Pharmacognosy. Homeopathy. Health food Pharmacology. Drug treatments Plant physiology and development Quercetin - pharmacology |
| title | Kinetics of Mushroom Tyrosinase Inhibition by Quercetin |
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