GDP-D-glucose phosphorylase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.7.78 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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GDP-D-glucose phosphorylase (EC 2.7.7.78) is an enzyme with systematic name GDP:alpha-D-glucose 1-phosphate guanylyltransferase. [1] This enzyme catalyses the following chemical reaction
The enzyme may be involved in prevention of misincorporation of glucose in place of mannose residues into glycoconjugates.
In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.
Glycogen phosphorylase is one of the phosphorylase enzymes. Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.
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.
Sucrose phosphorylase is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism.
In enzymology, a 1,3-beta-D-glucan phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a 1,3-beta-oligoglucan phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha,alpha-trehalose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha,alpha-trehalose phosphorylase (configuration-retaining) is an enzyme that catalyzes the chemical reaction
In enzymology, a cellobiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a kojibiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a laminaribiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a trehalose 6-phosphate phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an aldose-1-phosphate adenylyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an aldose-1-phosphate nucleotidyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a mannose-1-phosphate guanylyltransferase (GDP) is an enzyme that catalyzes the chemical reaction
Beta-D-galactosyl-(1->4)-L-rhamnose phosphorylase is an enzyme with systematic name beta-D-galactosyl-(1->4)-L-rhamnose:phosphate 1-alpha-D-galactosyltransferase. This enzyme catalyses the following chemical reaction
Nigerose phosphorylase is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-D-glucopyranose:phosphate beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction
N,N'-diacetylchitobiose phosphorylase is an enzyme with the systematic name N,N'-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase. This enzyme was found in the genus Vibrio initially but has now been found to be taken up by Escherichia coli as well as many other bacteria. One study shows that Escherichia coli can replicate on a medium that is just composed of GlcNAc a product of phosphorylation of N,N'-diacetylchitobiose as the sole source of carbon. Because E. coli can go on this medium, the enzyme is present. The enzyme has also been found in multiple eukaryotic cells as well, especially in eukaryotes that make chitin and break chitin down. It is believed that N,N'-diacetylchitobiose phosphorylase is an integral part of the phosphoenolpyruvate:glucose phosphotransferase system (PTS). It is assumed that it is involved with Enzyme Complex II of the PTS and is involved with the synthesis of chitin. The enzyme is specific for N,N'-diacetylchitobiose.
4-O-beta-D-mannosyl-D-glucose phosphorylase is an enzyme with systematic name 4-O-beta-D-mannopyranosyl-D-glucopyranose:phosphate alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction
3-O-alpha-D-glucosyl-L-rhamnose phosphorylase is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose:phosphate beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction