IRIS publication 5956761
Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.
RIS format for Endnote and similar
TY - JOUR - Paradisi F, Collins S, Maguire AR, Engel PC - 2007 - February - Journal of Biotechnology - Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives. - Validated - Altmetric: 1 () - 128 - 2 - 408 - 411 - Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts. - 10.1016/j.jbiotec.2006.08.008 DA - 2007/02 ER -
BIBTeX format for JabRef and similar
@article{V5956761, = {Paradisi F, Collins S and Maguire AR, Engel PC }, = {2007}, = {February}, = {Journal of Biotechnology}, = {Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.}, = {Validated}, = {Altmetric: 1 ()}, = {128}, = {2}, pages = {408--411}, = {{Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.}}, = {10.1016/j.jbiotec.2006.08.008}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Paradisi F, Collins S, Maguire AR, Engel PC | ||
YEAR | 2007 | ||
MONTH | February | ||
JOURNAL_CODE | Journal of Biotechnology | ||
TITLE | Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives. | ||
STATUS | Validated | ||
TIMES_CITED | Altmetric: 1 () | ||
SEARCH_KEYWORD | |||
VOLUME | 128 | ||
ISSUE | 2 | ||
START_PAGE | 408 | ||
END_PAGE | 411 | ||
ABSTRACT | Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts. | ||
PUBLISHER_LOCATION | |||
ISBN_ISSN | |||
EDITION | |||
URL | |||
DOI_LINK | 10.1016/j.jbiotec.2006.08.008 | ||
FUNDING_BODY | |||
GRANT_DETAILS |