Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.
Glucokinase belongs to the bacterial glucokinase family. Hexokinases phosphorylate glucose to produce glucose-6-phosphate, the first step in most glucose metabolism pathways. Alternative splicing of this gene results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, this enzyme is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI). It can Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage. It has a pivotal role as glucose sensor of the pancreatic beta-cells. Glucokinase of the beta-cell is induced or activated by glucose in contrast to liver glucokinase, which is regulated by insulin. Tissue-specific regulation corresponds with observations that liver and pancreatic beta-cell glucokinase are structurally distinct.
Glutamine Synthetase reglutes intracellular concentration of glutamate. Glutamine Synthetase catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is an important source of energy and that takes part in cell prolifetation, inhibition of apoptosis, and cell signaling. Glutamine Synthetase is expressed during early fetal stages, and has a role in maintaining body PH by removing ammonia from circulation. Mutations in the GLUL gene are related to congenital glutamine deficiency.
GLUT6 as a functionally uncharacterized transporter that putatively works in inflammatory responses. Inflammatory stimuli increase GLUT6 expression level, although GLUT6-knockout mice exhibit a subtle phenotype to lipopolysaccharide administration. Metabolomics and in vitro analyses show that GLUT6 functions as a glycolysis modulator in inflammatory macrophages. GLUT6 does not mediate glucose uptake and is localized on lysosomal membranes. We conclude that GLUT6 is a lysosomal transporter that is regulated by inflammatory stimuli and modulates inflammatory responses by affecting the metabolic shift in macrophages.
Glutamate Oxaloacetate Transaminase 1 (GOT1) is a cytoplasmic protein. GOT1 belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. GOT1 is a pyridoxal phosphate-dependent enzyme that exists in cytoplasmic and mitochondrial forms. GOT1 plays a key role in amino acid metabolism and the urea and tricarboxylic acid cycles. GOT1 involves in L-methionine salvage from methylthioadenosine, aspartate catabolic process, cellular response to insulin stimulus, polyamine metabolic process, and glucocorticoid stimulus.
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