PMID:3132906
| Citation |
Nagasawa, T, Ishii, T and Yamada, H (1988) Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149:413-6 |
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| Abstract |
D-Cysteine desulfhydrase of Escherichia coli W3110 delta trpED102/F' delta trpED102 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 alpha, beta-elimination reaction of O-acetyl-D-serine to form pyruvate, acetic acid and ammonia, but also the beta-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 (alpha, beta-elimination reaction) of 3-chloro-D-alanine, which is an effective antibacterial agent, E. coli W3110 delta trpED102/F' delta trpED102 did not show resistance against 3-chloro-D-alanine. Therefore, D-cysteine desulfhydrase does not contribute to 3-chloro-D-alanine detoxification in vivo. |
| Links | |
| Keywords |
Cystathionine gamma-Lyase/metabolism; Cysteine/biosynthesis; Cytosol/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Lyases/metabolism; Pseudomonas/enzymology; Serine/analogs & derivatives; Serine/metabolism; beta-Alanine/analogs & derivatives; beta-Alanine/metabolism |
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