Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cystathionine gamma-Lyase / chemistry
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Cystathionine gamma-Lyase / genetics*
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Cystathionine gamma-Lyase / metabolism*
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Cysteine / metabolism
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Cysteine Synthase
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Cystine / metabolism
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli / growth & development
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism*
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Gene Deletion
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Lyases
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Repressor Proteins
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Tryptophanase
Substances
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Escherichia coli Proteins
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Repressor Proteins
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MalY protein, E coli
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Cystine
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Cysteine Synthase
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Lyases
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Tryptophanase
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Cystathionine gamma-Lyase
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cystathionine beta-lyase
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Cysteine