Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Andreas C. Kleeb"'
Publikováno v:
Protein Engineering Handbook, Volume 1 & Volume 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::136760b3c1e635d41e4dc4e221a980f2
https://doi.org/10.1002/9783527634026.ch23
https://doi.org/10.1002/9783527634026.ch23
Publikováno v:
Biochimica et Biophysica Acta
The (13)C isotope effect for the conversion of prephenate to phenylpyruvate by the enzyme prephenate dehydratase from Methanocaldococcus jannaschii is 1.0334+/-0.0006. The size of this isotope effect suggests that the reaction is concerted. From the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfc90efdf22adcf1862879e26422eecb
Autor:
Andreas C. Kleeb, Martin Neuenschwander, Peter Kast, Lars Giger, Marianne Gamper, Maryam Hansson Edalat, Donald Hilvert, Johannes Haugstetter
The biosynthesis of small molecules can be fine-tuned by (re)engineering metabolic flux within cells. We have adapted this approach to optimize an in vivo selection system for the conversion of prephenate to phenylpyruvate, a key step in the producti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c39d331990e83b42c48786d60f2dd89
https://europepmc.org/articles/PMC1955800/
https://europepmc.org/articles/PMC1955800/
Publikováno v:
Biochemistry. 45(47)
Prephenate dehydratase (PDT) is an important but poorly characterized enzyme that is involved in the production of L-phenylalanine. Multiple-sequence alignments and a phylogenetic tree suggest that the PDT family has a common structural fold. On the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ad0ef4eaf8bb46451c89a3e57c9dc6f
https://pubmed.ncbi.nlm.nih.gov/17115705
https://pubmed.ncbi.nlm.nih.gov/17115705