Výsledky vyhledávání - "Jeffrey W. Munos"

Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C−H Activation by Soybean Lipoxygenase‐1

Autor: Shenshen Hu, Judith P. Klinman, Jérôme Cattin-Ortolá, 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

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Hydrolytic Enzymes as (Bio)-Logic for Wireless and Chipless Biosensors

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

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Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C-H Activation by Soybean Lipoxygenase-1

Autor: Shenshen Hu, Jérôme Cattin‐Ortolá, Jeffrey W. Munos, Judith P. Klinman

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

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Biosynthesis of Fosfomycin, Re-Examination and Re-Confirmation of a Unique Fe(II)- and NAD(P)H-Dependent Epoxidation Reaction

Autor: Hung Wen Liu, Jeffrey W. Munos, Pinghua Liu, Feng Yan

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

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A Secondary Kinetic Isotope Effect Study of the 1-Deoxy-d-xylulose-5-phosphate Reductoisomerase-catalyzed Reaction: Evidence for a Retroaldol-Aldol Rearrangement

Autor: Steven O. Mansoorabadi, Hak Joong Kim, Hung-wen Liu, Xiaotao Pu, Jeffrey W. Munos

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/

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Purification and Characterization of the Epoxidase Catalyzing the Formation of Fosfomycin from Pseudomonas syringae

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/

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Synthesis and analysis of a fluorinated product analogue as an inhibitor for 1-deoxy-D-xylulose 5-phosphate reductoisomerase

Autor: Hung-wen Liu, Jeffrey W. Munos, Xiaotao Pu

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

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Study of 1-deoxy-D-xylulose-5-phosphate reductoisomerase: synthesis and evaluation of fluorinated substrate analogues

Autor: Hung-wen Liu, Jeffrey W. Munos, Vidusha Devasthali, Kenneth A. Johnson, Alexander W. Wong

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

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