2017
DOI: 10.1016/j.ijbiomac.2017.04.014
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The light subunit of mushroom Agaricus bisporus tyrosinase: Its biological characteristics and implications

Abstract: The light subunit of mushroom Agaricus bisporus tyrosinase (LSMT) is a protein of unknown function that was discovered serendipitously during the elucidation of the crystal structure of the enzyme. The protein is non-immunogenic and can penetrate the intestinal epithelial cell barrier, and thus, similar to its structural homologue HA-33 from Clostridium botulinum, may be potentially absorbable by the intestine. LSMT also shares high structural homology with the ricin-B-like lectin from the mushroom Clitocybe n… Show more

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Cited by 23 publications
(26 citation statements)
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References 75 publications
(51 reference statements)
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“…Mushroom tyrosinase from Agaricus bisporus is a major and cheap enzyme, with high similarity and homology compared to human tyrosinase [1,37,38]. Due to the above-mentioned good properties, the structural, functional, and biochemical characteristics of mushroom tyrosinase have been studied extensively as a model system for screening of tyrosinase inhibitors and melanogenic studies, enzyme-catalyzed reactions, and enzyme-inhibitor structural studies so far [1,[39][40][41]. Tyrosinase from A. bisporus is a 120 kDa tetramer, which was first isolated by Bourquelot and Bertrand in 1895 [42].…”
Section: Tyrosinase and Its Key Role In Melanin Synthesismentioning
confidence: 99%
“…Mushroom tyrosinase from Agaricus bisporus is a major and cheap enzyme, with high similarity and homology compared to human tyrosinase [1,37,38]. Due to the above-mentioned good properties, the structural, functional, and biochemical characteristics of mushroom tyrosinase have been studied extensively as a model system for screening of tyrosinase inhibitors and melanogenic studies, enzyme-catalyzed reactions, and enzyme-inhibitor structural studies so far [1,[39][40][41]. Tyrosinase from A. bisporus is a 120 kDa tetramer, which was first isolated by Bourquelot and Bertrand in 1895 [42].…”
Section: Tyrosinase and Its Key Role In Melanin Synthesismentioning
confidence: 99%
“…Recently, a protein with a lectin-like structure was discovered [22] and named Abmb [37]. Interestingly, Abmb displays biological activities similar to lectins [20,38]. Abmb also has therapeutic potential [38]; hence, it is included in this review.…”
Section: Lectins and Lectin-like Protein In A Bisporusmentioning
confidence: 99%
“…Although human tyrosinase can be isolated from melanomas [ 6 , 7 , 8 ], well-defined preparations of recombinant hTyr with activities sufficient for large-scale inhibition studies have become available only in recent years [ 9 , 10 , 11 ]. Moreover, in the last decade, several X-ray structures of tyrosinases and tyrosinase-like proteins have been published, including mTyr [ 12 , 13 ], bacterial tyrosinases from Streptomyces castaneoglobisporus (sTyr, [ 14 ]) and Bacillus megaterium (bTyr, [ 15 ]), respectively, and, most recently, the human tyrosinase-related protein 1 (hTrp1), a melanogenic protein of yet unknown function in humans [ 16 ]. Common structural features of these proteins have been reviewed by several authors [ 17 , 18 , 19 ].…”
Section: Introductionmentioning
confidence: 99%