glucose-6-phosphate 1-epimerase | |||||||||
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Identifiers | |||||||||
EC no. | 5.1.3.15 | ||||||||
CAS no. | 37259-65-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glucose-6-phosphate 1-epimerase (EC 5.1.3.15) is an enzyme that catalyzes the chemical reaction
Hence, this enzyme has one substrate, alpha-D-glucose 6-phosphate, and one product, beta-D-glucose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is D-glucose-6-phosphate 1-epimerase. This enzyme participates in glycolysis / gluconeogenesis.
As of late 2013, 3 structures have been solved for this class of enzymes, with PDB accession codes 2CIQ, 2CIR, and 2CIS.
Galactose, sometimes abbreviated Gal, is a monosaccharide sugar that is about as sweet as glucose, and about 65% as sweet as sucrose. It is an aldohexose and a C-4 epimer of glucose. A galactose molecule linked with a glucose molecule forms a lactose molecule.
Isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:
Glucokinase is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver and pancreas of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia.
Galactokinase is an enzyme (phosphotransferase) that facilitates the phosphorylation of α-D-galactose to galactose 1-phosphate at the expense of one molecule of ATP. Galactokinase catalyzes the second step of the Leloir pathway, a metabolic pathway found in most organisms for the catabolism of α-D-galactose to glucose 1-phosphate. First isolated from mammalian liver, galactokinase has been studied extensively in yeast, archaea, plants, and humans.
Myophosphorylase or glycogen phosphorylase, muscle associated (PYGM) is the muscle isoform of the enzyme glycogen phosphorylase and is encoded by the PYGM gene. This enzyme helps break down glycogen into glucose-1-phosphate, so it can be used within the muscle cell. Mutations in this gene are associated with McArdle disease, a glycogen storage disease of muscle.
Phosphopentose epimerase encoded by the RPE gene is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.
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The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.
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Sucrose-phosphate synthase (SPS) is a plant enzyme involved in sucrose biosynthesis. Specifically, this enzyme catalyzes the transfer of a hexosyl group from uridine diphosphate glucose (UDP-glucose) to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate. This reversible step acts as the key regulatory control point in sucrose biosynthesis, and is an excellent example of various key enzyme regulation strategies such as allosteric control and reversible phosphorylation.
In enzymology, a trehalose 6-phosphate phosphorylase is an enzyme that catalyzes the chemical reaction