Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Denise A. Rock"'
Publikováno v:
Drug Metabolism and Disposition. 32:328-332
Quinoline was used to probe the steric and electronic contributions to rates of aromatic oxidation of nitrogen-containing, multiring substrates by cytochrome P450 (P450) enzymes. The regioselectivity of the P450 oxidation of quinoline was determined
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::047fdc120ff986e7dc26736dadefac16
https://doi.org/10.1124/dmd.32.3.328
https://doi.org/10.1124/dmd.32.3.328
Publikováno v:
Bioorganic Chemistry. 30:107-118
The substrate oxidation rates of P450 BM-3 are unparalleled in the cytochrome P450 (CYP) superfamily of enzymes. Furthermore, the bacterial enzyme, originating from Bacillus megaterium , has been used repeatedly as a model to study the metabolism of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e24c8b822da2e32de4afc88843c086d5
https://doi.org/10.1006/bioo.2002.1239
https://doi.org/10.1006/bioo.2002.1239
Autor:
Kevin J. French, Michael D. Strickler, Dan A. Rock, Denise A. Rock, Grace A. Bennett, Jan L. Wahlstrom, Barry M. Goldstein, Jeffrey P. Jones
Publikováno v:
Biochemistry. 40:9532-9538
This study examines the ability of P450cam to catalyze the formation of 2-ethylhexanoic acid from 2-ethylhexanol relative to its activity on the natural substrate camphor. As is the case for camphor, the P450cam exhibits stereoselectivity for binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8de38973e2cbceb9448504a8dd588f1
https://doi.org/10.1021/bi010063+
https://doi.org/10.1021/bi010063+
Publikováno v:
Biochemistry. 43(22)
The cytochrome P450 (CYP) isoforms involved in xenobiotic metabolism are enzymes whose substrate selectivity remains difficult to predict due to wide specificity and dynamic protein-substrate interactions. To uncover the determinants of specificity f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::675e289a03d42e5b835e003d2461b3a8
https://pubmed.ncbi.nlm.nih.gov/15170332
https://pubmed.ncbi.nlm.nih.gov/15170332
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 31(7)
Noncovalent forces, other than hydrophobic interactions, are important determinants of substrate bias exhibited by some cytochromes P450. The CYP2C9 pharmacophore is proposed to include either an anionic group or hydrogen bond donor in addition to it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::583107034feb1a5b7b8b41a7322f7c15
https://pubmed.ncbi.nlm.nih.gov/12814975
https://pubmed.ncbi.nlm.nih.gov/12814975
Publikováno v:
Journal of the American Chemical Society. 124(33)
Herein, we report the results from two experiments that are consistent with sulfoxidation and N-dealkylation involving two different enzyme substrate complexes and thus two different active oxygen species that do not interchange. The first experiment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::286cbe73b9c84ceccf43cf2808b1eea8
https://pubmed.ncbi.nlm.nih.gov/12175228
https://pubmed.ncbi.nlm.nih.gov/12175228
Autor:
Jeffrey P. Jones, Dan A. Rock, John I. Manchester, Denise A. Rock, Barry M. Goldstein, Kevin J. French
Publikováno v:
Archives of biochemistry and biophysics. 398(2)
Three factors are of primary importance with respect to designing efficient P450 biocatalysts. (1) The substrate must be oxidized at a significant rate. (2) The regioselectivity must heavily favor the desired product. (3) The enzyme must use the majo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72de5a140547753fd5a6384a8988a044
https://pubmed.ncbi.nlm.nih.gov/11831849
https://pubmed.ncbi.nlm.nih.gov/11831849
Publikováno v:
Journal of the American Chemical Society. 126:8868-8869
Multiple oxidants have been implicated as playing a role in cytochrome P450-mediated oxidations. Herein, we report results on N-dealkylation, one of the most facile reactions mediated by P450 enzymes. We have employed the N-oxides of a series of para
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3435828426b173e3a9424ef5555f5685
https://doi.org/10.1021/ja0486364
https://doi.org/10.1021/ja0486364
Publikováno v:
Protein Expression and Purification. 22:82-83
Two reductases, P450 oxidoreductase and P450Bm-3 reductase, were purified on a 2',5'-adenosine diphosphate solid support. Although the efficiency of these columns is well established, the cost of the resin and the eluting material 2'-adenosine can be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c08642411af0528d1ecac37c6384d5a
https://doi.org/10.1006/prep.2001.1385
https://doi.org/10.1006/prep.2001.1385