Zobrazeno 1 - 10
of 107
pro vyhledávání: '"Simon J. Pilkis"'
Summary The aim of this work was to investigate the role of fructose 2,6-bisphosphate (Fru 2,6-P2) during photosynthesis. The level of Fru 2,6-P2 in tobacco plants was elevated by the introduction of a modified mammalian gene encoding 6-phosphofructo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dbf2fd22c85a95fb299acc929d2ab71
https://ora.ox.ac.uk/objects/uuid:0734cb34-a024-4c57-ba5d-9b0e29a1dd98
https://ora.ox.ac.uk/objects/uuid:0734cb34-a024-4c57-ba5d-9b0e29a1dd98
Autor:
I. Deschamps, Graeme I. Bell, Philippe Passa, V. C. Pardini, Simon J. Pilkis, Irene T. Weber, Philippe Froguel, Gilberto Velho, C. Bellanné-Chantelot, Hélène Blanché, Jean-Jacques Robert, Martine Vaxillaire, Gregory M. Lipkind, D. Marotta, José Timsit
Publikováno v:
Diabetologia. 40:217-224
Mutations in glucokinase are associated with defects in insulin secretion and hepatic glycogen synthesis resulting in mild chronic hyperglycaemia, impaired glucose tolerance or diabetes mellitus. We screened members of 35 families with features of ma
Publikováno v:
Annual Review of Physiology. 58:171-186
The glycolytic enzyme glucokinase plays a key role in glucose sensing by the insulin-secreting pancreatic beta-cells, and mutations in the gene encoding this enzyme are a common cause of maturity-onset diabetes of the young (MODY), a form of non-insu
Autor:
M. Raafat El-Maghrabi, David A. Okar, Doriane Argaud, Alex J. Lange, Thomas C. Becker, Christopher B. Newgard, Simon J. Pilkis
Publikováno v:
Journal of Biological Chemistry. 270:24229-24236
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase has been postulated to be a metabolic signaling enzyme, which acts as a switch between glycolysis and gluconeogenesis in mammalian liver by regulating the level of fructose 2,6-bisphosphate. The ef
Publikováno v:
Biochemical and Biophysical Research Communications. 213:663-672
Arg-104 of the kinase domain of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase was mutated to alanine, the mutant enzyme expressed in E. coli with a T7 RNA polymerase-based expression system, and purified to homogeneity by Blue-Sepharose and Q-
Autor:
Simon J. Pilkis, Irwin J. Kurland
Publikováno v:
Protein Science. 4:1023-1037
The hepatic bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PF-2-K/Fru-2,6-P2ase), E.C. 2.7-1-105/E.C. 3-1-3-46, is one member of a family of unique bifunctional proteins that catalyze the synthesis and degradation of the
Publikováno v:
Annual Review of Biochemistry. 64:799-835
Publikováno v:
Journal of Biological Chemistry. 270:9939-9946
Glucokinase is distinguished from yeast hexokinase and low Km mammalian hexokinases by its low affinity for glucose and its cooperative behavior, even though glucose binding residues and catalytic residues are highly conserved in all of these forms o
Expression of Chicken Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase in Escherichia coli
Publikováno v:
Biochemical and Biophysical Research Communications. 209:883-893
Chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase was expressed in E. coli by using a pET3a T7 RNA polymerase-based expression system and was purified to homogeneity. The kinase and bisphosphatase of the expressed bifunctional enzyme
Publikováno v:
Journal of Biological Chemistry. 269:27458-27465
The determinants of sugar specificity and cooperative behavior of human beta-cell glucokinase were studied by mutating several active site residues and performing a steady-state kinetic analysis of the purified mutant and wild-type enzymes after thei