Identification and functional analysis of Escherichia coli cysteine desulfhydrases.
In Escherichia coli, three additional proteins having L-cysteine desulfhydrase activity were identified as O-acetylserine sulfhydrylase-A, O-acetylserine sulfhydrylase-B, and MalY protein, in addition to tryptophanase and cystathionine beta-lyase, which have been reported previously. The gene disruption for each protein was significantly effective for overproduction of L-cysteine and L-cystine. Growth phenotype and transcriptional analyses suggest that tryptophanase contributes primarily to L-cysteine degradation.
Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjojima, Matsuoka-cho, Fukui 910-1195, Japan.
Naoki
N
Awano
Masaru
M
Wada
Hirotada
H
Mori
Shigeru
S
Nakamori
Hiroshi
H
Takagi
D003542:Cystathionine gamma-Lyase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D003547:Cysteine Synthase; D003553:Cystine / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D017353:Gene Deletion; D008190:Lyases; D012097:Repressor Proteins; D014368:Tryptophanase
D029968:Escherichia coli Proteins; D012097:Repressor Proteins; C079405:MalY protein, E coli; D003553:Cystine; D003547:Cysteine Synthase; D008190:Lyases; D014368:Tryptophanase; D003542:Cystathionine gamma-Lyase; C019965:cystathionine beta-lyase; D003545:Cysteine