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• W1466732800 abstract "The chapter describes the enzymic methods for the preparation of L-tyrosine or its related amino acids. It reveals that β-tyrosinase catalyzes the synthesis of L-tyrosine or its related amino acids from DL-serine and phenol or its related compounds or from pyruvic acid, ammonia, and phenol or its related compounds, in significantly high yields. The chapter describes the physicochemical properties of β-tyrosinase. It examines the immobilization of various enzymes, which provide new approaches to elucidate the relation between the structure and function of enzymes, and gives new data for the practical application of enzymes. Apo- and holo-β-tyrosinases from Escherichia intermedia were covalently immobilized on cyanogen bromide (CNBr)-activated Sepharose. By the use of immobilized apo- β -tyrosinase on CNBr-activated Sepharose, its catalytic properties were examined. The immobilized enzyme reconstituted by pyridoxal phosphate lost its activity gradually when used repeatedly in a batch system without the addition of pyridoxal phosphate, but the initial activity was restored by a supplement of pyridoxal phosphate to the reaction system. The chapter concludes that β -tyrosinase was shown to catalyze a variety of α, β -elimination, β -replacement, and racemization reactions and the synthesis of L-tyrosine and its related amino acids." @default.
• W1466732800 created "2016-06-24" @default.
• W1466732800 creator A5011590619 @default.
• W1466732800 creator A5068552779 @default.
• W1466732800 date "1975-01-01" @default.
• W1466732800 modified "2023-10-10" @default.
• W1466732800 title "Synthesis of L-Tyrosine-Related Amino Acids by β-Tyrosinase" @default.
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• W1466732800 doi "https://doi.org/10.1016/s0065-2164(08)70431-3" @default.
• W1466732800 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1190012" @default.
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