Zobrazeno 1 - 10
of 87
pro vyhledávání: '"Thomas E. Roche"'
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Mammalian pyruvate dehydrogenase (PDH) activity is tightly regulated by phosphorylation and dephosphorylation, which is catalyzed by PDH kinase isomers and PDH phosphatase isomers, respectively. PDH phosphatase isomer 1 (PDP1) is a heterodimer consis
Autor:
Xinghong Dai, W.H Hui, Yasuaki Hiromasa, Z.H. Zhou, Thomas E. Roche, F.L Baiesc, Xuekui Yu, Jiansen Jiang
Publikováno v:
Biochemistry, vol 57, iss 16
Pyruvate dehydrogenase complex (PDC) is a large multienzyme complex that catalyzes the irreversible conversion of pyruvate to acetyl-coenzyme A with reduction of NAD+. Distinctive from PDCs in lower forms of life, in mammalian PDC, dihydrolipoyl acet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2998dd009556add6846605bdbe509ee1
https://escholarship.org/uc/item/8fq99111
https://escholarship.org/uc/item/8fq99111
Autor:
Yasuaki Hiromasa, Thomas E. Roche
Publikováno v:
Biochemistry. 47:2298-2311
In the complete absence of K+ and phosphate (Pi), pyruvate dehydrogenase kinase isoform 2 (PDHK2) was catalytically very active but with an elevated Km for ATP, and this activity is insensitive to effector regulation. We find that K+ or 5-fold lower
Autor:
Thorsten R. Knoechel, Peter J. Bungay, David Graham Brown, Thomas E. Roche, Alec D. Tucker, Colin M. Pfizer Global Res. Dev. Robinson, Chris Phillips, Wendy E. Pfizer Global Res. Dev. Taylor, Shane A. Kasten
Publikováno v:
Biochemistry. 45:402-415
Pyruvate dehydrogenase kinase (PDHK) regulates the activity of the pyruvate dehydrogenase multienzyme complex. PDHK inhibition provides a route for therapeutic intervention in diabetes and cardiovascular disorders. We report crystal structures of hum
Publikováno v:
Biochemistry. 43:15073-15085
Pyruvate dehydrogenase phosphatase isoform 1 (PDP1) is a heterodimer with a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). The activities of PDP1 or just PDP1c are greatly increased by Ca(2+)-dependent binding to the L2 (inner lipoyl) do
Publikováno v:
Journal of Biological Chemistry. 279:6921-6933
The subunits of the dihydrolipoyl acetyltransferase (E2) component of mammalian pyruvate dehydrogenase complex can form a 60-mer via association of the C-terminal I domain of E2 at the vertices of a dodecahedron. Exterior to this inner core structure
Autor:
Thomas E. Roche, Yasuaki Hiromasa
Publikováno v:
Journal of Biological Chemistry. 278:33681-33693
The dihydrolipoyl acetyltransferase (E2) has an enormous impact on pyruvate dehydrogenase kinase (PDK) phosphorylation of the pyruvate dehydrogenase (E1) component by acting as a mobile binding framework and in facilitating and mediating regulation o
Publikováno v:
Journal of Biological Chemistry. 277:14976-14985
The inner lipoyl domain (L2) of the dihydrolipoyl acetyltransferase (E2) 60-mer forms a Ca(2+)-dependent complex with the pyruvate dehydrogenase phosphatase 1 (PDP1) or its catalytic subunit, PDP1c, in facilitating large enhancements of the activitie
Autor:
Thomas E. Roche, M. Eric Gershwin, Yasuni Nakanuma, Jean Francois Bach, Patrick S.C. Leung, Judith A Van de Water, Motoko Sasaki, Aftab A. Ansari, Neil Pumford, Ross L. Coppel, Ken M. Humphries, Luke I. Szweda
Publikováno v:
Journal of Autoimmunity. 15:51-60
Previous studies documenting the existence of cross-reactivity between the lipoated (but not unlipoated) forms of the inner lipoyl domain (E2L2) of PDC-E2 [the major autoantigen in Primary biliary cirrhosis (PBC)] and trifluoroacetylated (TFA) protei
Autor:
Tao Peng, Stephen J. Yeaman, Alexander Yakhnin, Xiaoming Gong, Michal Zolkiewski, Janet Quinn, Thomas E. Roche
Publikováno v:
Journal of Biological Chemistry. 275:13645-13653
Efficient catalysis in the second step of the pyruvate dehydrogenase (E1) component reaction requires a lipoyl group to be attached to a lipoyl domain that displays appropriately positioned specificity residues. As substrates, the human dihydrolipoyl