Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Alexandra N. Bogner"'
Autor:
Ashley C. Campbell, Thomas P. Quinn, Austin R. Prater, Alexandra N. Bogner, Kent S. Gates, Donald F. Becker, John J. Tanner
Publikováno v:
ACS Chem Biol
Proline dehydrogenase (PRODH) is a flavoenzyme that catalyzes the first step of proline catabolism, the oxidation of L-proline to Δ(1)-pyrroline-5-carboxylate. PRODH has emerged as a cancer therapy target because of its involvement in the metabolic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a70f8c8ae94af37561b34329db3fb63
https://doi.org/10.1021/acschembio.1c00427
https://doi.org/10.1021/acschembio.1c00427
Acinetobacter baumannii is a Gram-negative opportunistic pathogen that causes nosocomial infections, especially among immunocompromised individuals. The rise of multidrug resistant strains of A. baumannii has limited the use of standard antibiotics,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6ce33ebad2239afb7eb07809f9532ad
https://hdl.handle.net/10919/113361
https://hdl.handle.net/10919/113361
Publikováno v:
Biochemistry. 61(22)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::498e0644d86a030048d0a914ac6008c8
https://pubmed.ncbi.nlm.nih.gov/36314559
https://pubmed.ncbi.nlm.nih.gov/36314559
Publikováno v:
Protein Sci
Aldehyde dehydrogenase 4A1 (ALDH4A1) catalyzes the final steps of both proline and hydroxyproline catabolism. It is a dual substrate enzyme that catalyzes the NAD(+)‐dependent oxidations of L‐glutamate‐γ‐semialdehyde to L‐glutamate (prolin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cf9f3f8504021ce411b1d405631c2c8
https://doi.org/10.1002/pro.4131
https://doi.org/10.1002/pro.4131
Publikováno v:
Protein engineering, designselection : PEDS. 35
Proline dehydrogenase (PRODH) catalyzes the FAD-dependent oxidation of l-proline to Δ1-pyrroline-5-carboxylate and is a target for inhibitor discovery because of its importance in cancer cell metabolism. Because human PRODH is challenging to purify,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b24795f10b5c3df3d1e41f18902e93d
https://pubmed.ncbi.nlm.nih.gov/36448708
https://pubmed.ncbi.nlm.nih.gov/36448708
Autor:
John J. Tanner, Gabriela S. Tam, Anke Vandekeere, Alexandra N. Bogner, Sagar M. Patel, Emily M. Christensen, Donald F. Becker, Sarah-Maria Fendt
Publikováno v:
Journal of Biological Chemistry
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the biosynthetic half-reaction of the proline cycle by reducing Δ1-pyrroline-5-carboxylate (P5C) to proline through the oxidation of NAD(P)H. Many cancers alter their proline metabolism by up-reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01d1f0867fe7a0a3900fc23d93d6e2a4
https://doi.org/10.1074/jbc.ra120.016106
https://doi.org/10.1074/jbc.ra120.016106
Publikováno v:
Amino Acids
Proline metabolism features prominently in the unique metabolism of cancer cells. Proline biosynthetic genes are consistently upregulated in multiple cancers, while the proline catabolic enzyme proline dehydrogenase has dual, context-dependent pro-ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46f4403f132c0c7b1b0a9905d4ce0a03
https://europepmc.org/articles/PMC8599497/
https://europepmc.org/articles/PMC8599497/
Publikováno v:
Arch Biochem Biophys
Proline utilization A (PutA) proteins are bifunctional proline catabolic enzymes that catalyze the 4-electron oxidation of L-proline to L-glutamate using spatially-separated proline dehydrogenase and L-glutamate-γ-semialdehyde dehydrogenase (GSALDH,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd55e098f98ed0f5667be0c22fdb4546
https://europepmc.org/articles/PMC7856085/
https://europepmc.org/articles/PMC7856085/