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The biochemistry and molecular biology of the glucose-6-phosphatase system Foster JD; Nordlie RCExp Biol Med (Maywood) 2002[Sep]; 227 (8): 601-8Progress has continued to be made over the past 4 years in our understanding of the glucose-6-phosphatase (G6Pase) system. The gene for a second component of the system, the putative glucose-6-P transporter (G6PT), was cloned, and mutations in this gene were found in patients diagnosed with glycogen storage disease type 1b. The functional characterization of this putative G6PT has been initiated, and the relationship between substrate transport via the G6PT and catalysis by the system's catalytic subunit continues to be explored. A lively debate over the feasibility of various aspects of the two proposed models of the G6Pase system persists, and the functional/structural relationships of the individual components of the system remain a hot topic of interest in G6Pase research. New evidence supportive of physiologic roles for the biosynthetic functions of the G6Pase system in vivo also has emerged over the past 4 years.|Amino Acid Sequence[MESH]|Animals[MESH]|Antiporters/genetics/physiology[MESH]|Catalysis[MESH]|Catalytic Domain[MESH]|Diabetes Mellitus, Type 2/enzymology[MESH]|Glucose-6-Phosphatase/chemistry/genetics/*physiology[MESH]|Glucose-6-Phosphate/metabolism[MESH]|Glucose/metabolism[MESH]|Glycogen Storage Disease Type I/enzymology/genetics[MESH]|Humans[MESH]|Mice[MESH]|Mice, Knockout[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Monosaccharide Transport Proteins/genetics/physiology[MESH]|Phosphates/metabolism[MESH]|Phosphorylation[MESH]|Protein Conformation[MESH]|Protein Subunits[MESH]|Recombinant Fusion Proteins/physiology[MESH]|Structure-Activity Relationship[MESH] |
