Zobrazeno 1 - 10
of 53
pro vyhledávání: '"David C. LaPorte"'
Publikováno v:
Journal of Biological Chemistry. 278:26450-26457
GSY1 is one of the two genes encoding glycogen synthase in Saccharomyces cerevisiae. Both the GSY1 message and the protein levels increased as cells approached stationary phase. A combination of deletion analysis and site-directed mutagenesis reveale
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::069254225bb2fd6024d6429c078ea425
https://doi.org/10.1074/jbc.m211808200
https://doi.org/10.1074/jbc.m211808200
Publikováno v:
Journal of Biological Chemistry. 277:7567-7573
In Escherichia coli, the homodimeric Krebs cycle enzyme isocitrate dehydrogenase (EcIDH) is regulated by reversible phosphorylation of a sequestered active site serine. The phosphorylation cycle is catalyzed by a bifunctional protein, IDH kinase/phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f77320bab5239cdab96937ce564b9979
https://doi.org/10.1074/jbc.m107908200
https://doi.org/10.1074/jbc.m107908200
Publikováno v:
Journal of Biological Chemistry. 276:26154-26163
Isocitrate dehydrogenase from Bacillus subtilis (BsIDH) is a member of a family of metal-dependent decarboxylating dehydrogenases. Its crystal structure was solved to 1.55 A and detailed comparisons with the homologue from Escherichia coli (EcIDH), t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f5da9c8d6b68624c989b71608d6bcde
https://doi.org/10.1074/jbc.m101191200
https://doi.org/10.1074/jbc.m101191200
Autor:
C. Oudot, C. Blanchet, A. Di Pietro, J. C. Cortay, David C. LaPorte, J M Jault, A. J. Cozzone
Publikováno v:
Biochemistry. 40:3047-3055
The isocitrate dehydrogenase kinase/phosphatase (IDHK/P) of E. coli is a bifunctional enzyme responsible for the reversible phosphorylation of isocitrate dehydrogenase (IDH) on a seryl residue. As such, it belongs to the serine/threonine protein kina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41977c5f9b216dd2758a3719ca3f54df
https://doi.org/10.1021/bi001713x
https://doi.org/10.1021/bi001713x
Publikováno v:
Yeast. 18:1505-1514
Yeast glycogen metabolism responds to environmental stressors such as nutrient limitation and heat shock. This response is mediated, in part, by the regulation of the glycogen metabolic genes. Environmental stressors induce a number of glycogen metab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b83c0c2046eadef125ec1bd3777e6bb0
https://doi.org/10.1002/yea.752
https://doi.org/10.1002/yea.752
Autor:
Elizabeth J. Karschnia, Charles Romfo, Stephen P. Miller, Ridong Chen, David C. LaPorte, Antony M. Dean
Publikováno v:
Journal of Biological Chemistry. 275:833-839
Isocitrate dehydrogenase (IDH)(1) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase. In this paper, we demonstrate that the effectors controlling these activities belong to two distinct classes that differ in mechanis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2d7cddbd7231cdbe51e34f18572de97
https://doi.org/10.1074/jbc.275.2.833
https://doi.org/10.1074/jbc.275.2.833
Autor:
Elizabeth J. Karschnia, Graeme I. Bell, David C. LaPorte, Gulshan R. Anand, Stephen P. Miller, Alex J. Lange
Publikováno v:
Diabetes. 48:1645-1651
Glucokinase (GK) is expressed in the pancreatic beta-cells and liver, and plays a key role in the regulation of glucose homeostasis. The enzymatic activity and thermal stability of wild-type (WT) GK and several mutant forms associated with maturity-o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a2e8fb9af24d8462c3daf4c1a80e1ad
https://doi.org/10.2337/diabetes.48.8.1645
https://doi.org/10.2337/diabetes.48.8.1645
Autor:
Diana B. Cherbavaz, David C. LaPorte, Susan E. Tsutakawa, Daniel E. Koshland, Robert M. Stroud, Janet Finer-Moore
Publikováno v:
Biochemistry. 36:13890-13896
To clarify further the mechanism of regulation by phosphorylation of isocitrate dehydrogenase, cocrystallization of isocitrate dehydrogenase and isocitrate dehydrogenase kinase/phosphatase in the presence of an ATP analog was attempted. Although cocr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa48b8135e5a4fef27c966a86888db1
https://doi.org/10.1021/bi9711691
https://doi.org/10.1021/bi9711691
Publikováno v:
Journal of Bacteriology. 178:4704-4709
The control of the glyoxylate bypass operon (aceBAK) of Escherichia coli is mediated by two regulatory proteins, IclMR and FadR. IclMR is a repressor protein which has previously been shown to bind to a site which overlaps the aceBAK promoter. FAR is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f18bb79d0bd20ef5c4652d33c324e20f
https://doi.org/10.1128/jb.178.15.4704-4709.1996
https://doi.org/10.1128/jb.178.15.4704-4709.1996
Publikováno v:
Journal of Biological Chemistry. 271:19124-19128
Isocitrate dehydrogenase (IDH) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase. In addition to the kinase and phosphatase activities, this protein catalyzes an intrinsic ATPase reaction. The initial velocity kinetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07b6326d7bc67831fd7ea7345b6f7b73
https://doi.org/10.1074/jbc.271.32.19124
https://doi.org/10.1074/jbc.271.32.19124