Physiological comparison ofd-cysteine desulfhydrase ofEscherichia coliwith 3-chloro-d-alanine dehydrochlorinase ofPseudomonas putidaCR 1-1

✍ Scribed by Toru Nagasawa; Takafumi Ishii; Hideaki Yamada

• Book ID: 104770352
• Publisher: Springer
• Year: 1988
• Tongue: English
• Weight: 467 KB
• Volume: 149
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00425580

✦ Synopsis

D-Cysteine desulfhydrase of Escherichia coli W3110 AtrpEDlO2/F'AtrpEDl02 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 c~,fl-elimination reaction of O-acetyl-D-serine to form pyruvate, acetic acid and ammonia, but also the/?-replacement reaction of Oacetyl-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 (~,/?-elimination reaction) of 3-chloro-D-alanine, which is an effective antibacterial agent, E. coli W3110 AtrpEDIO2/F'AtrpEDI02 did not show resistance against 3-chloro-D-alanine. Therefore, D-cysteine desulfhydrase does not contribute to 3-chloro-Dalanine detoxification in vivo.