Papain catalysed hydantoin hydrolysis in the synthesis of amino acids.
Papain has been shown, for the first time, to exhibit hydantoinase activity. It hydrolyzes the 5-mono and 5,5'-disubstituted hydantoins with linear and cyclic substituents, with a higher activity for the latter, to the corresponding N-carbamoyl amino acids, which on chemical hydrolysis yield the corresponding amino acids. The up-scaling of this simple procedure could be a major break-through for amino acid synthesis in chemical and pharmaceutical industries.
Rai
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Department of Biochemistry, Faculty of Science, Banaras Hindu University, Varanasi, India. taneja@banaras.ernet.in
Taneja
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D000581:Amidohydrolases / Q000378:metabolism*; D000596:Amino Acids / Q000096:biosynthesis*; D002617:Chemical Industry; D004345:Drug Industry; D006827:Hydantoins / Q000378:metabolism*; D006868:Hydrolysis; D010206:Papain / Q000378:metabolism*; D013379:Substrate Specificity
D000596:Amino Acids; D006827:Hydantoins; D010206:Papain; D000581:Amidohydrolases; C020047:dihydropyrimidinase