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pro vyhledávání: '"Tina M. Knox"'
Autor:
Charles G. Miller, Maria E. Carinato, Christopher A. Conlin, Patricia Collin-Osdoby, Tina M. Knox, Xioming Yang
Publikováno v:
Journal of Bacteriology. 180:3517-3521
Salmonella typhimurium apeR mutations lead to overproduction of an outer membrane-associated N -acetyl phenylalanine β-naphthyl ester-cleaving esterase that is encoded by the apeE gene (P. Collin-Osdoby and C. G. Miller, Mol. Gen. Genet. 243:674–6
Two well-characterized enzymes in Salmonella enterica serovar Typhimurium and Escherichia coli are able to hydrolyze N-terminal aspartyl (Asp) dipeptides: peptidase B, a broad-specificity aminopeptidase, and peptidase E, an Asp-specific dipeptidase.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9211d12ab37ba180c28b7028c3476d0
https://europepmc.org/articles/PMC95209/
https://europepmc.org/articles/PMC95209/
Publikováno v:
Journal of bacteriology. 182(12)
Peptidase B (PepB) of Salmonella enterica serovar Typhimurium is one of three broad-specificity aminopeptidases found in this organism. We have sequenced the pepB gene and found that it encodes a 427-amino-acid (46.36-kDa) protein, which can be unamb
The Salmonella typhimurium pepT gene is induced nearly 30-fold in response to anaerobiosis. Anaerobic expression is dependent on the transcriptional regulator encoded by fnr (previously oxrA). Primer extension analysis and site-directed mutagenesis e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::751ccbb972787662eb852c4cfddcfc82
https://europepmc.org/articles/PMC178913/
https://europepmc.org/articles/PMC178913/
Cloning and physical map position of an alpha-aspartyl dipeptidase gene, pepE, from Escherichia coli
Publikováno v:
Journal of bacteriology. 176(5)