Zobrazeno 1 - 10
of 86
pro vyhledávání: '"Verne, Schirch"'
Publikováno v:
Frontiers in Pharmacology, Vol 10 (2019)
Neonatal epileptic encephalopathy (NEE), as a result of pyridoxine 5′-phosphate oxidase (PNPO) deficiency, is a rare neural disorder characterized by intractable seizures and usually leads to early infant death. The clinical phenotypes do not respo
Externí odkaz:
https://doaj.org/article/474b0acd662b4cfb8ed17af118e60f85
Autor:
Amit K Gandhi, Jigar V Desai, Mohini S Ghatge, Martino L di Salvo, Stefano Di Biase, Richmond Danso-Danquah, Faik N Musayev, Roberto Contestabile, Verne Schirch, Martin K Safo
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e40954 (2012)
Several drugs and natural compounds are known to be highly neurotoxic, triggering epileptic convulsions or seizures, and causing headaches, agitations, as well as other neuronal symptoms. The neurotoxic effects of some of these compounds, including t
Externí odkaz:
https://doaj.org/article/59c7c18da118465ba193a6194bf54281
Autor:
Mohini S Ghatge, Roberto Contestabile, Martino L di Salvo, Jigar V Desai, Amit K Gandhi, Christina M Camara, Rita Florio, Isabel N González, Alessia Parroni, Verne Schirch, Martin K Safo
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e41680 (2012)
Pyridoxal 5'-phosphate (PLP) is a cofactor for dozens of B(6) requiring enzymes. PLP reacts with apo-B(6) enzymes by forming an aldimine linkage with the ε-amino group of an active site lysine residue, thus yielding the catalytically active holo-B(6
Externí odkaz:
https://doaj.org/article/120dee9975ab43af9abb54d72c3321d4
Autor:
Mostafa H. Ahmed, Sayali S. Karve, Kendra Cunningham, Verne Schirch, Martin K. Safo, Tanya M. S. David, Mohini S. Ghatge, Faik N. Musayev
Publikováno v:
FEBS Open Bio
Pyridoxal 5'-phosphate (PLP) is a cofactor for many vitamin B6-requiring enzymes that are important for the synthesis of neurotransmitters. Pyridoxine 5'-phosphate oxidase (PNPO) is one of two enzymes that produce PLP. Some 16 known mutations in huma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddde947fc6234c77d18188b2eeefbbad
http://europepmc.org/articles/PMC4856418
http://europepmc.org/articles/PMC4856418
Autor:
Mario A. Saavedra, Martin K. Safo, Roberto Contestabile, Mohini S. Ghatge, Verne Schirch, Faik N. Musayev, Martino L. di Salvo, Alexina C. Haynes
Publikováno v:
Journal of Biological Chemistry. 284:30949-30956
Mutations in pyridoxine 5'-phosphate oxidase are known to cause neonatal epileptic encephalopathy. This disorder has no cure or effective treatment and is often fatal. Pyridoxine 5'-phosphate oxidase catalyzes the oxidation of pyridoxine 5'-phosphate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34f5ba3edfff3ffbc853ea9c2f7538d2
https://doi.org/10.1074/jbc.m109.038372
https://doi.org/10.1074/jbc.m109.038372
Autor:
Martino L. di Salvo, Martin K. Safo, Samuel O. Aboagye, Mohini S. Ghatge, Faik N. Musayev, Amit Gandhi, Aaron Sease, Verne Schirch
Publikováno v:
Biochemical and Biophysical Research Communications. 381:12-15
Pyridoxal kinase catalyzes the phosphorylation of pyridoxal (PL) to pyridoxal 5'-phosphate (PLP). A D235A variant shows 7-fold and 15-fold decreases in substrate affinity and activity, respectively. A D235N variant shows approximately 2-fold decrease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eea5c6a6f33b21941866a5dd36b34e37
https://doi.org/10.1016/j.bbrc.2009.01.170
https://doi.org/10.1016/j.bbrc.2009.01.170
Autor:
Faik N. Musayev, Martin K. Safo, Verne Schirch, Martino L. di Salvo, Amit Gandhi, Tzu-Ping Ko, Ashwini Goswami
Publikováno v:
Protein Science. 16:2184-2194
Pyridoxal kinase catalyzes the transfer of a phosphate group from ATP to the 5' alcohol of pyridoxine, pyridoxamine, and pyridoxal. In this work, kinetic studies were conducted to examine monovalent cation dependence of human pyridoxal kinase kinetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cbe163635418a9963fae92245da8024
https://doi.org/10.1110/ps.073022107
https://doi.org/10.1110/ps.073022107
Publikováno v:
Archives of Biochemistry and Biophysics. 442:92-101
Serine hydroxymethyltransferase (SHMT) is a key enzyme in the formation and regulation of the folate one-carbon pool. Recent studies on human subjects have shown the existence of two single nucleotide polymorphisms that may be associated with several
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e8ccedc3e6929863019abee27ce54c9
https://doi.org/10.1016/j.abb.2005.07.018
https://doi.org/10.1016/j.abb.2005.07.018
Autor:
Doletha M. E. Szebenyi, Verne Schirch
Publikováno v:
Current Opinion in Chemical Biology. 9:482-487
Recent structural data and the properties of several active site mutants of serine hydroxymethyltransferase have resolved some key questions concerning the catalytic mechanism and broad substrate specificity of this enzyme. In the tetrahydrofolate-de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a2148660074afcc798f2c03896050e6
https://doi.org/10.1016/j.cbpa.2005.08.017
https://doi.org/10.1016/j.cbpa.2005.08.017
Publikováno v:
Protein Expression and Purification. 36:300-306
Pyridoxal kinase is an ATP dependent enzyme that phosphorylates pyridoxal, pyridoxine, and pyridoxamine forming their respective 5'-phosphorylated esters. The kinase is a part of the salvage pathway for re-utilizing pyridoxal 5'-phosphate, which serv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fc27d28fc76b2d3f1f9a750077fa610
https://doi.org/10.1016/j.pep.2004.04.021
https://doi.org/10.1016/j.pep.2004.04.021