|
type |
Journal Article |
authors |
Nagasawa, T.; Ishii, T.; Yamada, H. |
title |
Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1 |
journal |
Arch Microbiol |
Activity |
4.4.1.15 |
ui |
88251237 |
year |
(1988) |
volume |
149 |
number |
5 |
pages |
413-6 |
| |
keywords |
Comparative Study |
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. |
last changed |
2004/02/13 17:51 |
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