Enzymatic synthesis of l-cysteine by O-acetylserine sulfhydrylase of 3-chloro-l-alanine resistant Bacillus sphaericus L-118 |
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Authors: | Toru Nagasawa Gurdev Singh Dhillon Takafumi Ishii Hideaki Yamada |
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Affiliation: | Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Sakyo-Ku, Kyoto 606, Japan |
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Abstract: | The regulatory properties of serine-O-transacetylase and O-acetylserine sulfhydrylase have been investigated with 3-chloro-l-alanine resistant Bacillus sphaericus L-118. The enhancement of O-acetylserine sulfhydrylase formation by 3-chloro-l-alanine was observed and this effect was counteracted by corepressor l-cysteine. O-Acetylserine sulfhydrylase occurring in B. sphaericus L-118 can catalyse β-replacement reaction of 3-chloro-l-alanine in the presence of a high concentration of sodium hydrosulfide to form l-cysteine. The optimal reaction conditions for l-cysteine production were studied using resting cells. Under optimal conditions, about 80% of the added 3-chloro-l-alanine could be converted to l-cysteine. The highest yield achieved was 70 mg of l-cysteine per 1.0 ml of the reaction mixture. |
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