Výsledky vyhledávání - "F. Scott Mathews"

The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase

Autor: Jian-Hua Gan, Jie Li, Zong-Xiang Xia, F. Scott Mathews

Publikováno v: Biochemical and Biophysical Research Communications. 406:621-626

Methanol dehydrogenase is a heterotetrameric enzyme containing the prosthetic group pyrroloquinoline quinone (PQQ), which catalyzes the oxidation of methanol to formaldehyde. The crystal structure of methanol dehydrogenase from Methylophilus W3A1, pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbe8bc513f9147e95762ecde23c8128a
https://doi.org/10.1016/j.bbrc.2011.02.107

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Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein Interface

Autor: F. Scott Mathews, Moonsung Choi, Narayanasami Sukumar, Victor L. Davidson, Aimin Liu

Publikováno v: Biochemistry. 50:1265-1273

Amicyanin is a type 1 copper protein that serves as an electron acceptor for methylamine dehydrogenase (MADH). The site of interaction with MADH is a "hydrophobic patch" of amino acid residues including those that comprise a "ligand loop" that provid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::731b7f645d903e5c8f7290769580bb4b
https://doi.org/10.1021/bi101794y

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Structural Characterization of Mutations at the Oxygen Activation Site in Monomeric Sarcosine Oxidase

Autor: F. Scott Mathews, Zhi-wei Chen, Marilyn Schuman Jorns

Publikováno v: Biochemistry. 49:3631-3639

Oxygen reduction and sarcosine oxidation in monomeric sarcosine oxidase (MSOX) occur at separate sites above the si- and re-faces, respectively, of the flavin ring. Mutagenesis studies implicate Lys265 as the oxygen activation site. Substitution of L

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bf003c3852f7fbdcfa4537640faaf4a
https://doi.org/10.1021/bi100160j

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Factors That Affect Oxygen Activation and Coupling of the Two Redox Cycles in the Aromatization Reaction Catalyzed by NikD, an Unusual Amino Acid Oxidase

Autor: Marilyn Schuman Jorns, Robert C. Bruckner, Phaneeswara Rao Kommoju, F. Scott Mathews, Patricia Ferreira, Christopher J. Carrell

Publikováno v: Biochemistry. 48:9542-9555

NikD is a flavoprotein oxidase that catalyzes the oxidation of piperideine-2-carboxylate (P2C) to picolinate in a remarkable aromatization reaction comprising two redox cycles and at least one isomerization step. Tyr258 forms part of an "aromatic cag

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::052dbf2a253598f6f5c24adf37f9347f
https://doi.org/10.1021/bi901056a

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Crystal and molecular structure of tert. -butyloxycarbonyl-L-prolyl-α-aminoisobutyryl-L-alanyl-α-aminoisobutyrate methyl ester

Autor: F. Scott Mathews, Garland R. Marshall, Edmund W. Czerwinski, Patrick Van Roey, T. M. Balasubramanian, G. David Smith

Publikováno v: International Journal of Peptide and Protein Research. 22:404-409

Boc-Pro-Aib-Ala-Aib-OMe crystallizes in the orthorhombic space group P2(1)2(1)2 with cell dimensions a = 17.701 (3) A, b = 17.476 (4) A, c = 9.686 (2) A, V = 2996.3 A3. The first three residues form a single turn of a 3(10)-helix stabilized by two in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2af07cd79081cfe35c1285d461fa908
https://doi.org/10.1111/j.1399-3011.1983.tb02109.x

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Structural identification of the pathway of long-range communication in an allosteric enzyme

Autor: Prafull S. Gandhi, Zhi-wei Chen, F. Scott Mathews, Enrico Di Cera

Publikováno v: Proceedings of the National Academy of Sciences. 105:1832-1837

Allostery is a common mechanism of regulation of enzyme activity and specificity, and its signatures are readily identified from functional studies. For many allosteric systems, structural evidence exists of long-range communication among protein dom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a93420e44a97df193865868177ab137
https://doi.org/10.1073/pnas.0710894105

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Important Role of the Cys-191–Cys-220 Disulfide Bond in Thrombin Function and Allostery

Autor: Agustin O. Pineda, Leslie A. Bush-Pelc, Francesca Marino, Zhi-wei Chen, F. Scott Mathews, Enrico Di Cera

Publikováno v: Journal of Biological Chemistry. 282:27165-27170

Little is known on the role of disulfide bonds in the catalytic domain of serine proteases. The Cys-191-Cys-220 disulfide bond is located between the 190 strand leading to the oxyanion hole and the 220-loop that contributes to the architecture of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e810ddc4744044d20e6de7ceb695f5e
https://doi.org/10.1074/jbc.m703202200

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