|
type |
Journal Article |
authors |
Wada, M., Awano, N., Haisa, K., Takagi, H., Nakamori, S. |
title |
Purification, characterization and identification of cysteine desulfhydrase of Corynebacterium glutamicum, and its relationship to cysteine production |
journal |
FEMS Microbiol Lett |
Activity |
4.4.1.28 |
Family |
4.4.1.28.a |
sel |
selected |
ui |
12445652 |
year |
(2002) |
volume |
217 |
number |
1 |
pages |
103-107 |
| |
abstract |
We highly purified the enzyme having L-cysteine desulfhydrase activity from Corynebacterium glutamicum. According to its partial amino acid sequence, the enzyme was identified as the aecD gene product, a C-S lyase with alpha, beta-elimination activity [I. Rossol and A. Puhler (1992) J. Bacteriol. 174, 2968-2977]. To produce L-cysteine in C. glutamicum, the Escherichia coli-altered cysE gene encoding Met256Ile mutant serine acetyltransferase, which is desensitized to feedback inhibition by L-cysteine, was introduced into C. glutamicum. When the altered cysE gene was expressed in the aecD-disrupted strain, the transformants produced approximately 290 mg of L-cysteine plus L-cystine per liter from glucose. The produced amount of these amino acids was about two-fold higher than that of the wild-type strain.
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last changed |
2017/09/08 10:12 |
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