Výsledky vyhledávání - "Breeanna Mintmier"

NUDT7 regulates total hepatic CoA levels and the composition of the intestinal bile acid pool in male mice fed a Western diet

Autor: Schuyler D. Vickers, Stephanie A. Shumar, Dominique C. Saporito, Amina Kunovac, Quincy A. Hathaway, Breeanna Mintmier, Judy A. King, Rachel D. King, Vazhaikkurichi M. Rajendran, Aniello M. Infante, John M. Hollander, Roberta Leonardi

Publikováno v: The Journal of biological chemistry. 299(1)

Nudix hydrolase 7 (NUDT7) is an enzyme that hydrolyzes CoA species, is highly expressed in the liver, and resides in the peroxisomes. Peroxisomes are organelles where the preferential oxidation of dicarboxylic fatty acids occurs and where the hepatic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::528e6a48032181237073ef012b024559
https://pubmed.ncbi.nlm.nih.gov/36436558

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Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: a case study with periplasmic nitrate reductase

Autor: Jennifer M McGarry, Breeanna Mintmier, Partha Basu, Daniel J. Bain

Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 26:13-28

The molybdopterin enzyme family catalyzes a variety of substrates and plays a critical role in the cycling of carbon, nitrogen, arsenic, and selenium. The dimethyl sulfoxide reductase (DMSOR) subfamily is the most diverse family of molybdopterin enzy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45acdd98ba160c093e69ee2722bfcdc4
https://doi.org/10.1007/s00775-020-01833-9

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Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation

Autor: Breeanna Mintmier, Samih Nassif, Partha Basu, John F. Stolz

Publikováno v: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 25(4)

Mononuclear molybdenum enzymes catalyze a variety of reactions that are essential in the cycling of nitrogen, carbon, arsenic, and sulfur. For decades, the structure and function of these crucial enzymes have been investigated to develop a fundamenta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9474756f8e69af84218f86b65d42bbeb
https://pubmed.ncbi.nlm.nih.gov/32279136

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Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni

Autor: Jennifer M McGarry, Joseph Sallmen, Joseph R. McCormick, Partha Basu, Breeanna Mintmier, Günter Schwarz, John F. Stolz, Daniel J. Bain, Courtney Sparacino-Watkins, Axel Magalon, Katrin Fischer-Schrader

Publikováno v: FEMS Microbiology Letters
FEMS Microbiology Letters, Wiley-Blackwell, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩
FEMS Microbiology Letters, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩

Campylobacter jejuni, a human gastrointestinal pathogen, uses nitrate for growth under microaerophilic conditions using periplasmic nitrate reductase (Nap). The catalytic subunit, NapA, contains two prosthetic groups, an iron sulfur cluster and a mol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d8372ac5f1fedbb92c3ecc337d6310e
https://hal-amu.archives-ouvertes.fr/hal-01919478

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