Výsledky vyhledávání - "Eduardo, Vottero"

Active site substitution a82w improves the regioselectivity of steroid hydroxylation by cytochrome p450 bm3 mutants as rationalized by spin relaxation nuclear magnetic resonance studies

Autor: Sybren S. Wijmenga, Eduardo Vottero, Vanina Rea, Ard J. Kolkman, Nico P. E. Vermeulen, Kirsten A.M. Ampt, Jan N. M. Commandeur, E.J. Stronks, Maarten Honing

Publikováno v: Biochemistry, 51, 750-760
Biochemistry, 51(3), 750-760. American Chemical Society
Rea, V, Kolkman, A J, Vottero, E R, Stronks, E J, Ampt, K A, Honing, M, Vermeulen, N P E, Wijmenga, S S & Commandeur, J N M 2012, ' Active Site Substitution A82W Improves the Regioselectivity of Steroid Hydroxylation by Cytochrome P450 BM3 Mutants As Rationalized by Spin Relaxation Nuclear Magnetic Resonance Studies ', Biochemistry, vol. 51, no. 3, pp. 750-760 . https://doi.org/10.1021/bi201433h
Biochemistry, 51, 3, pp. 750-760

Cytochrome P450 BM3 from Bacillus megaterium is a monooxygenase with great potential for biotechnological applications. In this paper, we present engineered drug-metabolizing P450 BM3 mutants as a novel tool for regioselective hydroxylation of steroi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6516bb58e7de7294bb79663245d3cb7
https://doi.org/10.1021/bi201433h

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Insights into regioselective metabolism of mefenamic acid by cytochrome P450 BM3 mutants through crystallography, docking, molecular dynamics, and free energy calculations

Autor: Luigi, Capoferri, Rasmus, Leth, Ernst, ter Haar, Arun K, Mohanty, Peter D J, Grootenhuis, Eduardo, Vottero, Jan N M, Commandeur, Nico P E, Vermeulen, Flemming Steen, Jørgensen, Lars, Olsen, Daan P, Geerke

Publikováno v: Proteins. 84(3)

Cytochrome P450 BM3 (CYP102A1) mutant M11 is able to metabolize a wide range of drugs and drug-like compounds. Among these, M11 was recently found to be able to catalyze formation of human metabolites of mefenamic acid and other nonsteroidal anti-inf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7b35a65c2db683bdce86441f2f40966f
https://pubmed.ncbi.nlm.nih.gov/26757175

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Inhibitors of human indoleamine 2,3-dioxygenase identified with a target-based screen in yeast

Autor: Aruna D. Balgi, Michel Roberge, Katherine Woods, A. Grant Mauk, Stuart Tugendreich, Teri Melese, Eduardo Vottero, Raymond J. Andersen

Publikováno v: Biotechnology Journal. 1:282-288

Indoleamine 2,3-dioxygenase (IDO) is a tryptophan degradation enzyme that is emerging as an important drug target. IDO is expressed by many human tumors to help them escape immune detection, and it has been implicated in depression and in the formati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f9689a2d6f47e8464503efeddc7b0f
https://doi.org/10.1002/biot.200600001

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Application of a fluorescence-based continuous-flow bioassay to screen for diversity of cytochrome P450 BM3 mutant libraries

Autor: Jan N. M. Commandeur, Eduardo Vottero, Jelle Reinen, Suilan Ferman, Nico P. E. Vermeulen

Publikováno v: Reinen, J, Ferman, S, Vottero, E R, Vermeulen, N & Commandeur, J N M 2011, ' Application of a fluorescence-based continuous-flow bioassay to screen for diversity of cytochrome P450 BM3 mutant libraries ', Journal of Biomolecular Screening, vol. 16, no. 2, pp. 239-250 . https://doi.org/10.1177/1087057110394180
Journal of Biomolecular Screening, 16(2), 239-250. SAGE Publications Inc.

A fluorescence-based continuous-flow enzyme affinity detection (EAD) setup was used to screen cytochrome P450 BM3 mutants on-line for diversity. The flow-injection screening assay is based on the BM3-mediated O-dealkylation of alkoxyresorufins formin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::077f835401ae863b5f21aef0dc236776
https://pubmed.ncbi.nlm.nih.gov/21297109

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Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua

Autor: Harry C, Brastianos, Eduardo, Vottero, Brian O, Patrick, Rob, Van Soest, Teatulohi, Matainaho, A Grant, Mauk, Raymond J, Andersen

Publikováno v: Journal of the American Chemical Society. 128(50)

Exiguamine A (1), a hexacyclic alkaloid with an unprecedented skeleton, has been isolated from the marine sponge Neopetrosia exigua collected in Papua New Guinea. The structure of exiguamine A (1) was elucidated by a combination of spectroscopic anal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8b57a5a7a4f67a0926a53f80f27ab3d4
https://pubmed.ncbi.nlm.nih.gov/17165752

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Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific Marine Hydroid Garveia annulata

Autor: Raymond J. Andersen, Michel Roberge, Alban R. Pereira, A. Grant Mauk, Eduardo Vottero

Publikováno v: Journal of natural products. 69(10)

Crude extracts of the marine hydroid Garveia annulata show potent inhibition of indoleamine 2,3-dioxygenase (IDO). Fractionation of the extract led to the identification of the new polyketides annulin C (1), 2-hydroxygarveatin E (4), garveatin E (5),

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4660771e1125414abf8192fb4d431b63
https://pubmed.ncbi.nlm.nih.gov/17067170

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Exiguamine A., an Indoleamine-2,3-dioxygenase (IDO) Inhibitor Isolated from the Marine Sponge Neopetrosia exigua

Autor: Eduardo Vottero, Rob W. M. Van Soest, Raymond J. Andersen, Harry C. Brastianos, Teatulohi Matainaho, A. Grant Mauk, Brian O. Patrick

Publikováno v: Journal of the American Chemical Society, 128, 16046-16047. American Chemical Society

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::110fcc43370866638501aae5fc7a5a5d
https://dare.uva.nl/personal/pure/en/publications/exiguamine-a-an-indoleamine23dioxygenase-ido-inhibitor-isolated-from-the-marine-sponge-neopetrosia-exigua(8f2c5633-65ab-4ff6-b064-67d6bde63985).html

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Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11

Autor: Nico P. E. Vermeulen, Vanina Rea, Jeroen Lastdrager, Maarten Honing, Eduardo Vottero, Jan N. M. Commandeur

Publikováno v: Journal of Biological Inorganic Chemistry-JBIC, 16(6), 899-912. Springer Verlag
Vottero, E R, Rea, V, Lastdrager, J, Honing, M, Vermeulen, N P E & Commandeur, J N M 2011, ' Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11 ', Journal of Biological Inorganic Chemistry-JBIC, vol. 16, no. 6, pp. 899-912 . https://doi.org/10.1007/s00775-011-0789-4
Journal of Biological Inorganic Chemistry

CYP102A1, originating from Bacillus megaterium, is a highly active enzyme which has attracted much attention because of its potential applicability as a biocatalyst for oxidative reactions. Previously we developed drug-metabolizing mutant CYP102A1 M1

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Cytochrome b5 is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast

Autor: Michel Roberge, Ivan Sadowski, Michael J. Page, Ross T. A. MacGillivray, David A. Mitchell, Eduardo Vottero, A. Grant Mauk

Publikováno v: FEBS Letters. (9):2265-2268

The evolutionary relationship of indoleamine 2,3-dioxygenase (IDO) to some gastropod myoglobins suggests thatIDO may undergo autoxidation in vivo such that one or morecurrently unidentiﬁed electron donors are required to maintainIDO heme iron in th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52928b8b2b87cffcf8e2a24b5d8550a8

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