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- W1569134572 abstract "The acetyl ester of homoserine was found to be an intermediate in methionine biosynthesis in fungi, where it plays the role that O-succinylhomoserine does in bacteria. The latter is formed from succinyl coenzyme A and homoserine, and is decomposed by the replacement of succinate by cysteine to yield cystathionine. When grown in the presence of labeled homoserine, Neurospora accumulated labeled O-acetylhomoserine as well as larger amounts of the α-hydroxy analogue. A methionine-requiring mutant, me-5, which could grow when given acetylhomoserine in place of methionine, failed to accumulate it or to form labeled cystathionine when grown with labeled homoserine. A sensitive assay for hydroxyamino acid-acylating enzymes was devised, utilizing the observation that these enzymes catalyze exchange between alcohol and ester. Extracts of yeast and Neurospora were shown to catalyze homoserine exchange only with acetylhomoserine; extracts of Salmonella, only with succinylhomoserine. Homoserine acetylase was purified 60-fold from Neurospora. Acetyl-CoA could not be replaced by acetyl derivatives of phosphate, carnitine, or acyl carrier protein. The exchange rate was not affected by end product methionine. Although not leaky nutritionally, the me-5 mutant appears to produce a modified enzyme able to catalyze net acetylation but not exchange. Extracts of both fungi and bacteria can utilize either the succinyl or the acetyl ester of homoserine for cystathionine synthesis. In Salmonella this is due to the low specificity of the cystathionine γ-synthetase, but cystathionine synthesis from succinylhomoserine in Neurospora appears to be catalyzed by γ-cystathionase." @default.
- W1569134572 created "2016-06-24" @default.
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- W1569134572 date "1967-09-01" @default.
- W1569134572 modified "2023-09-28" @default.
- W1569134572 title "Acetylhomoserine" @default.
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- W1569134572 doi "https://doi.org/10.1016/s0021-9258(18)95831-x" @default.
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