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Tyrosine aminotransferase, induced in Trichoderma viride by l-tyrosine, was isolated from the culture medium, partially purified and characterized. The enzyme was inducible by both l- and dl-tyrosine, although l-tyrosine was the better inducer. The enzyme required l-tyrosine and a-ketoglutarate as amino donor and amino acceptor, respectively. Its pH optimum in 50 mm-potassium phosphate buffer was 7·6, the apparent Michaelis constants were 0·5 mm for l-tyrosine and 0·25 mm for a-ketoglutarate; it had a molecular weight of 110000.
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