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Agricultural and Biological Chemistry
Vol. 46 (1982) No. 12 P 2967-2977

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http://doi.org/10.1271/bbb1961.46.2967


Five aminotransferases, TA-A, -B, -T, -PI, -PII, which might participate in the biosyntheses of aspartate, branched-chain amino acids, tyrosine, and phenylalanine, respectively, were separated from one another in Brevibacterium flavum, and examined for their keto-acid substrate specificities and the apparent Michaelis constants (Km') for their main substrates. TA-A specifically reacted with oxalacetate, among the keto-acids tested, and accounted for 90% of the total activity in the cellular extracts. TA-B was found to be the only aminotransferase that reacted with branchedchain keto-acids, and also showed some activity with prephenate and phenylpyruvate but having a much larger Km' than the other enzymes. TA-T specifically reacted with prephenate and oxalacetate, among the keto-acids tested, and accounted for 80 and 2% of the total activities of the cellular extracts, respectively, but showed a much larger Km' for oxalacetate than did TA-A. TA-PI and -PII showed similar substrate-specificities and Km's to each other. They were active with phenylpyruvate, p-hydroxylphenylpyruvate, prephenate, and oxalacetate. Their activity with phenylpyruvate accounted for only 36% of the total activity, but showed a markedly smaller Km' than did TA-B having 64% of the total activity. An aspartate auxotroph, No. 102-7, was found to lack TA-A and TA-PI, and to have a reduced amount of TA-PII. The relative activity of the mutant TA-PII with oxalacetate decreased to about 1/10 that of the wild-type TA-PII. Two groups (I and II) of prototrophic revertants were derived from No. 102-7: Group I restored TA-A but neither TA-PI nor TA-PII, while group II restored none of the three enzymes but had a new type of aminotransferase which was active with aspartate, but showed different chromatographic properties from TA-A.

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