Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jeffrey W. Munos"'
Publikováno v:
Angewandte Chemie International Edition. 55:9361-9364
The ability to relate a hierarchy of protein motions to function remains a compelling experimental challenge at the interface of chemistry and biology. In particular, the proposed contribution of distinctly different classes of local vs. global prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f80868b48d6e76c545aff99bcd235449
https://doi.org/10.1002/anie.201603592
https://doi.org/10.1002/anie.201603592
Autor:
Mehrdad Mehdizadeh, Joseph C. McAuliffe, Nigel F. Reuel, RuPing Wang, Jeffrey W. Munos, William J. Delaney, Gregory A. Becht
Publikováno v:
ACS Sensors. 1:348-353
The switchable activity of allosteric, hydrolytic enzymes was used as a single-input, “buffer” logic gate (performing YES and NOT) in a screen-printable biosensor. The enzyme substrate functioned as an “AND” logic gate with the enzyme and cof
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d377c94cf3b0d1537a56642b924ff776
https://doi.org/10.1021/acssensors.5b00259
https://doi.org/10.1021/acssensors.5b00259
Publikováno v:
Angewandte Chemie (International ed. in English), vol 55, iss 32
The proposed contributions of distinct classes of local versus global protein motions during enzymatic bond making/breaking processes has been difficult to verify. We employed soybean lipoxygenase-1 as a model system to investigate the impact of high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8412fc7deb3776760f01fa6ae170406c
https://escholarship.org/uc/item/57n716t4
https://escholarship.org/uc/item/57n716t4
Publikováno v:
Biochemistry. 45:11473-11481
(S)-2-hydroxypropylphosphonic acid epoxidase (HppE) catalyzes the epoxide ring closure of (S)-HPP to form fosfomycin, a clinically useful antibiotic. Early investigation showed that its activity can be reconstituted with Fe(II), FMN, NADH, and O2, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95303954823d530d668d03bd9837bb81
https://doi.org/10.1021/bi060839c
https://doi.org/10.1021/bi060839c
1-Deoxy-d-xylulose 5-phosphate (DXP) reductoisomerase (DXR, also known as methyl-d-erythritol 4-phosphate (MEP) synthase) is a NADPH-dependent enzyme, which catalyzes the conversion of DXP to MEP in the nonmevalonate pathway of isoprene biosynthesis.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f5aa49e64c6128c1b655b6ffbcb7825
https://europepmc.org/articles/PMC2650392/
https://europepmc.org/articles/PMC2650392/
Autor:
Jeffrey W. Munos, Lin Hong, Hung-wen Liu, Feng Yan, Wei-Chen Chang, Aimin Liu, Sung-Ju Moon, Steven O. Mansoorabadi
The final step in the biosynthesis of fosfomycin in Streptomyces wedmorensis is catalyzed by ( S)-2-hydroxypropylphosphonic acid (HPP) epoxidase ( Sw-HppE). A homologous enzyme from Pseudomonas syringae whose encoding gene ( orf3) shares a relatively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f253080fdc58bbb4d97ef1ee96618ff6
https://europepmc.org/articles/PMC2780581/
https://europepmc.org/articles/PMC2780581/
Publikováno v:
Bioorganicmedicinal chemistry letters. 18(10)
1-Deoxy- d -xylulose 5-phosphate (DXP) reductoisomerase (DXR) is an NADPH-dependent enzyme catalyzing the rearrangement and reduction of DXP to methyl- d -erythritol 4-phosphate (MEP). Two mechanisms for this enzymatic reaction have been proposed, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::538e7f30b3fc3d35ef04eeb781aeeb8e
https://pubmed.ncbi.nlm.nih.gov/18078746
https://pubmed.ncbi.nlm.nih.gov/18078746
Publikováno v:
Organic letters. 6(20)
[reaction: see text] 1-deoxy-D-xylulose-5-phosphate (DXP) reductoisomerase is a NADPH-dependent enzyme catalyzing the conversion of DXP to methyl-D-erythritol 4-phosphate (MEP). In this study, each of the hydroxyl groups in DXP and one of its C-1 hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea09d5095e9ddac0ececc8e38e3bb4d3
https://pubmed.ncbi.nlm.nih.gov/15387564
https://pubmed.ncbi.nlm.nih.gov/15387564
Autor:
Hu, Shenshen1, Cattin ‐ Ortolá, Jérôme1,2, Munos, Jeffrey W.1,3, Klinman, Judith P.1,4 klinman@berkeley.edu
Publikováno v:
Angewandte Chemie. 8/1/2016, Vol. 128 Issue 32, p9507-9510. 4p.