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Physiological comparison of d-cysteine desulfhydrase of Escherichia coli with 3-chloro-d-alanine dehydrochlorinase of Pseudomonas putida CR 1-1

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Abstract

d-Cysteine desulfhydrase of Escherichia coli W3110 ΔtrpED102/F′ ΔtrpED102 was physiologically characterized. It was found to be located in the cytosolic fraction, as 3-chloro-d-alanine dehydrochlorinase is. d-Cysteine desulfhydrase catalyzed not only the α,β-elimination reaction of O-acetyl-d-serine to form pyruvate, acetic acid and ammonia, but also the β-replacement reaction of O-acetyl-d-serine with sulfide to form d-cysteine. However, these reactions appeared not to proceed in vivo. No other activity of d-cysteine synthesis from O-acetyl-d-serine and sulfide was detected in a crude cell extract of E. coli which was immunotitrated with antibodies raised against the purified d-cysteine desulfhydrase. Although d-cysteine desulfhydrase catalyzes the degradation (α,β-elimination reaction) of 3-chloro-d-alanine, which is an effective antibacterial agent, E. coli W3110 ΔtrpED102/F′ ΔtrpED102 did not show resistance against 3-chloro-d-alanine. Therefore, d-cysteine desulfhydrase does not contribute to 3-chloro-d-alanine detoxification in vivo.

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Authors and Affiliations

  1. Department of Agricultural Chemistry, Kyoto University, 606, Kyoto, Japan

    Toru Nagasawa, Takafumi Ishii & Hideaki Yamada

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  1. Toru Nagasawa
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  2. Takafumi Ishii
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  3. Hideaki Yamada
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Nagasawa, T., Ishii, T. & Yamada, H. Physiological comparison of d-cysteine desulfhydrase of Escherichia coli with 3-chloro-d-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149, 413–416 (1988). https://doi.org/10.1007/BF00425580

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  • DOI: https://doi.org/10.1007/BF00425580

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