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Fish tyrosinase enzyme involved in melanin biosynthesis: Insights from physicochemical characterization, homology modeling, and virtual screening studies.

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Title Fish tyrosinase enzyme involved in melanin biosynthesis: Insights from physicochemical characterization, homology modeling, and virtual screening studies.
Not Available
 
Creator Kumari, R., Jahageerdar, S., Panche, A, Sanath Kumar
 
Subject Transmembrane region; hydrophobicity; extinction coefficient; expasy; virtual screening
 
Description Not Available
In the vertebrates, including fish, the tyrosinase enzyme plays an essential role in coloration. Modulation of tyrosinase activity is expected to alter the body pigmentation in fish and other vertebrate species. In the present study, physicochemical, functional, and structural properties of tyrosinase of three fish species viz., goldfish, Japanese medaka, and common carp were determined. The homology model was developed using the Chimera1.1.2, Swiss model, and Phyre2, and the best model was selected upon evaluation. Further, a virtual screening method was applied to identify the putative modulators using the PyRx- Virtual screening tool. The estimated physicochemical and functional properties of tyrosinase from the three species suggested that they all are hydrophobic, acidic, thermostable, with a high extinction coefficient (Cys, Trp, and Tyr) and have transmembrane-segment. Based on virtual screening against 13,000 compounds from the zinc database, five compounds were determined as potent modulators of fish tyrosinase with a binding energy of 7.0 to 8.8 Kcal/ mol. Of these, Pilosine (ZINC13469966) was found to be the best putative modulator with low binding energy and properties of standardized drugs. This study showed that the tyrosinase
function could be modulated to alter the pigment formation in fish species by using
small compound.
Not Available
 
Date 2022-06-16T04:47:27Z
2022-06-16T04:47:27Z
2020-01-01
 
Type Research Paper
 
Identifier Not Available
Not Available
http://krishi.icar.gov.in/jspui/handle/123456789/72598
 
Language English
 
Relation Not Available;
 
Publisher Taylor & Francis