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- W2080510501 abstract "Tryptophan synthase (M.W. 150000) of Neurospora crassa is shown to be a dimeric enzyme consisting of two identical polypeptides of 75000 daltons. The amino-termini of the enzyme are not reactive with dansyl chloride even when the protein is unfolded prior to dansylation. End-group analysis with carboxy-peptidase A revealed that phenylalanine and leucine are released most rapidly; however, the kinetic results seem to account for two chains with an identical carboxyl-terminal sequence - Leu · Phe · COOH. These findings, taken together with the genetic data, suggest that although the enzyme is bifunctional it is the product of a single structural gene which has evolved through a mechanism of gene-fusion." @default.
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- W2080510501 date "1965-03-01" @default.
- W2080510501 modified "2023-10-11" @default.
- W2080510501 title "Chemical and physical studies of the structure of tryptophan synthetase from Neurospora crassa" @default.
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- W2080510501 doi "https://doi.org/10.1016/0006-291x(65)90865-x" @default.
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