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CDP-glucose + glycogenin
CDP + glucosylated glycogenin
-
recombinant enzyme expressed in E. coli, 71% activity compared to UDP-glucose
-
?
CDP-glucose + p-nitrophenyl-alpha-maltoside
CDP + ?
-
recombinant enzyme expressed in E. coli
-
-
?
TDP-glucose + glycogenin
TDP + glucosylated glycogenin
-
recombinant enzyme expressed in E. coli, 33% activity compared to UDP-glucose
-
?
TDP-glucose + p-nitrophenyl-alpha-maltoside
TDP + ?
-
recombinant enzyme expressed in E. coli
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-galactose + glycogenin
UDP + galactosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
UDP-glucose + glycogenin
UDP + glucosylglycogenin
UDP-glucose + maltose
UDP + maltotriose
trans-glucosylation. 93% of the transferred glucose molecules appears in maltotriose, 6% are attached to glycogenin, and 1% is liberated as free glucose
-
-
?
UDP-glucose + N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
UDP + glucosylated N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
UDP-glucose + n-octyl-alpha-D-maltoside
?
UDP-glucose + n-octyl-beta-D-maltoside
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
UDP-xylose + n-dodecyl-beta-D-maltoside
?
-
transglucosylation reaction
-
-
?
additional information
?
-
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
self-glucosylation of the glycosyltransferase glycogenin
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
UDP-glucose can not be replaced by ADP- or GDP-glucose
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
glucose molecule is attached to Tyr-194
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
glucosylation reaches a plateau, when 5 additional glucose residues have been added to glycogenin, i.e. primed glycogenin
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
i.e. unprimed glycogenin
glucosylation reaches a plateau, when 5 additional glucose residues have been added to glycogenin, i.e. primed glycogenin
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
no activity with UDP-N-acetylglucosamine and GDP-mannose
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
regulation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue by autoglycosylation, catalyzes two chemically different autoglucosylation reactions, the glucosylation of a tyrosine hydroxyl group and the formation of alpha-1,4 glucosidic linkages by subsequent glucosylations
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
one attached glucose molecule is needed for intramolecular self-glucosylation
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
no activity with CDP-glucose
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
UDP-glucose can not be replaced by ADP- or GDP-glucose
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
regulation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
-
increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. Glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
self-glucosylating initiator of glycogen synthesis
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
self-glucosylation
-
-
?
UDP-glucose + N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
UDP + glucosylated N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
-
simultaneously and independently of the autoglycosylation reaction
-
-
?
UDP-glucose + N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
UDP + glucosylated N-(maltosyl-alpha-1,4-(1-deoxyglucitol))-peptide
-
peptide sequence: SISIYSYLP
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
renal enzyme
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
transglucosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
transglucosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
simultaneously and independently of the autoglycosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
transglucosylation reaction
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
simultaneously and independently of the autoglycosylation reaction
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
-
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
simultaneously and independently of the autoglycosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
-
transglucosylation reaction
-
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
-
transglucosylation reaction
-
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
-
-
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
-
autoglycosylation reaction
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
-
renal and skeletal muscle glycogenin, lower activity compared to UDP-glucose
-
?
additional information
?
-
-
glycogenin-1 catalyzes both the glucose-O-tyrosine linkage and the alpha1,4 glucosidic bonds linking the glucose molecules in the oligosaccharide
-
-
?
additional information
?
-
human glycogenin during its reaction cycle shows a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This switch includes the ordering of a polypeptide stretch containing Tyr195, and major movement of an approximately 30-residue lid segment covering the active site. The rearranged lid guides the nascent maltosaccharide chain into the active site in either an intra- or intersubunit mode dependent upon chain length and steric factors and positions the donor and acceptor sugar groups for catalysis. Mapping of donor and acceptor subsites in hGYG1, overview
-
-
?
additional information
?
-
-
human glycogenin during its reaction cycle shows a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This switch includes the ordering of a polypeptide stretch containing Tyr195, and major movement of an approximately 30-residue lid segment covering the active site. The rearranged lid guides the nascent maltosaccharide chain into the active site in either an intra- or intersubunit mode dependent upon chain length and steric factors and positions the donor and acceptor sugar groups for catalysis. Mapping of donor and acceptor subsites in hGYG1, overview
-
-
?
additional information
?
-
glycosylated HLPFIYNLSSNTMYTYSPAFK peptide products originating from glycogenin-2, mass spectrometric analysis, overview
-
-
?
additional information
?
-
glycosylated HLPFIYNLSSNTMYTYSPAFK peptide products originating from glycogenin-2, mass spectrometric analysis, overview
-
-
?
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
-
no activity with nonapeptide SISIYSYLP and N-lactosylated peptide
-
-
?
additional information
?
-
OsGGT-gene expression increases in FR13A (a submergence-tolerant cultivar, Indica) during submergence but decreases in IR42 (submergence-intolerant cultivar, Indica). The expression of the OsGGT gene in FR13A is induced by salicylic acid and benzyladenine. The accumulation of OsGGT mRNA in FR13A also increases in response to ethylene, gibberellin, abscisic acid, drought and salt treatment, but methyl jasmonate treatment and cold stress have no effect on expression. OsGGT gene can be related to submergence stress and associated with a general defensive response to various environmental stresses
-
-
?
additional information
?
-
-
OsGGT-gene expression increases in FR13A (a submergence-tolerant cultivar, Indica) during submergence but decreases in IR42 (submergence-intolerant cultivar, Indica). The expression of the OsGGT gene in FR13A is induced by salicylic acid and benzyladenine. The accumulation of OsGGT mRNA in FR13A also increases in response to ethylene, gibberellin, abscisic acid, drought and salt treatment, but methyl jasmonate treatment and cold stress have no effect on expression. OsGGT gene can be related to submergence stress and associated with a general defensive response to various environmental stresses
-
-
?
UDP-alpha-D-glucose + glycogenin
additional information
-
-
-
after 60 min of incubation the glycogenin molecules possess an average glucosyl chain length of 11.3 residues
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
UDP-glucose + glycogenin
UDP + glucosylglycogenin
additional information
?
-
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
regulation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue by autoglycosylation, catalyzes two chemically different autoglucosylation reactions, the glucosylation of a tyrosine hydroxyl group and the formation of alpha-1,4 glucosidic linkages by subsequent glucosylations
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
enzyme forms the protein part of proteoglycogen
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
regulation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
the glycogenin subunit of glycogen synthase, EC 2.4.1.11, catalyzes this reaction, i.e. the enzyme catalyzes its own glucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
-
increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. Glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
self-glucosylating initiator of glycogen synthesis
-
-
?
additional information
?
-
OsGGT-gene expression increases in FR13A (a submergence-tolerant cultivar, Indica) during submergence but decreases in IR42 (submergence-intolerant cultivar, Indica). The expression of the OsGGT gene in FR13A is induced by salicylic acid and benzyladenine. The accumulation of OsGGT mRNA in FR13A also increases in response to ethylene, gibberellin, abscisic acid, drought and salt treatment, but methyl jasmonate treatment and cold stress have no effect on expression. OsGGT gene can be related to submergence stress and associated with a general defensive response to various environmental stresses
-
-
?
additional information
?
-
-
OsGGT-gene expression increases in FR13A (a submergence-tolerant cultivar, Indica) during submergence but decreases in IR42 (submergence-intolerant cultivar, Indica). The expression of the OsGGT gene in FR13A is induced by salicylic acid and benzyladenine. The accumulation of OsGGT mRNA in FR13A also increases in response to ethylene, gibberellin, abscisic acid, drought and salt treatment, but methyl jasmonate treatment and cold stress have no effect on expression. OsGGT gene can be related to submergence stress and associated with a general defensive response to various environmental stresses
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,4-alpha-glucan branching enzyme deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Cardiomyopathies
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
Cardiomyopathies
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Cardiomyopathies
Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage.
Diabetes Mellitus
The role of glycogenin in glycogen synthesis and non-insulin dependent diabetes mellitus.
Diabetes Mellitus, Type 2
Mutational analysis of the coding regions of the genes encoding protein kinase B-alpha and -beta, phosphoinositide-dependent protein kinase-1, phosphatase targeting to glycogen, protein phosphatase inhibitor-1, and glycogenin: lessons from a search for genetic variability of the insulin-stimulated glycogen synthesis pathway of skeletal muscle in NIDDM patients.
Glycogen Storage Disease
A new muscle glycogen storage disease associated with glycogenin-1 deficiency.
Glycogen Storage Disease
A newly identified c.1824_1828dupATACG mutation in exon 13 of the GAA gene in infantile-onset glycogen storage disease type II (Pompe disease).
Glycogen Storage Disease
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
Glycogen Storage Disease
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Glycogen Storage Disease
Glycogen and its metabolism: some new developments and old themes.
Glycogen Storage Disease
Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
Glycogen Storage Disease
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
Glycogen Storage Disease
Molecular pathogenesis of a new glycogenosis caused by a glycogenin-1 mutation.
Glycogen Storage Disease
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
Glycogen Storage Disease
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.
Glycogen Storage Disease Type II
A newly identified c.1824_1828dupATACG mutation in exon 13 of the GAA gene in infantile-onset glycogen storage disease type II (Pompe disease).
glycogenin glucosyltransferase deficiency
A new muscle glycogen storage disease associated with glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
glycogenin glucosyltransferase deficiency
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
glycogenin glucosyltransferase deficiency
Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage.
glycogenin glucosyltransferase deficiency
Glycogenin-1 deficiency and inactivated priming of glycogen synthesis.
glycogenin glucosyltransferase deficiency
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
glycogenin glucosyltransferase deficiency
Muscle glycogen synthesis and breakdown are both impaired in glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Polyglucosan myopathy and functional characterization of a novel GYG1 mutation.
glycogenin glucosyltransferase deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
HIV Infections
Peripheral blood RNA gene expression in children with pneumococcal meningitis: a prospective case-control study.
Lafora Disease
Glycogen and its metabolism: some new developments and old themes.
Lafora Disease
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Muscle Weakness
Severe asymmetric muscle weakness revealing glycogenin-1 polyglucosan body myopathy.
Muscular Diseases
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Muscular Diseases
GYG1: A distal myopathy with polyglucosan bodies.
Muscular Diseases
Late-onset polyglucosan body myopathy in five patients with a homozygous mutation in GYG1.
Muscular Diseases
Longitudinal follow-up and muscle MRI pattern of two siblings with polyglucosan body myopathy due to glycogenin-1 mutation.
Muscular Diseases
Muscle pathology and whole-body MRI in a polyglucosan myopathy associated with a novel glycogenin-1 mutation.
Muscular Diseases
Polyglucosan myopathy and functional characterization of a novel GYG1 mutation.
Muscular Diseases
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Muscular Diseases
Severe asymmetric muscle weakness revealing glycogenin-1 polyglucosan body myopathy.
Muscular Dystrophies, Limb-Girdle
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
Neoplasms
Metastasis of Uveal Melanoma with Monosomy-3 Is Associated with a Less Glycogenetic Gene Expression Profile and the Dysregulation of Glycogen Storage.
Perinatal Death
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
Respiratory Distress Syndrome
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
ring-type e3 ubiquitin transferase deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Sarcoma, Ewing
Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism.
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evolution
-
glycogenin is a member of the GT8 family of glycosyltransferases with a GT-A architecture
evolution
the Pacific oyster has three isozymes of glycogenin: CgGN-alpha, CgGN-beta, and CgGN-gamma. Functional motif architecture analysis shows that CgGN is structurally similar to mammalian glycogenin-1. All three CgGN isoforms contain the key domain of glycosyltransferase and the C-terminal domain
evolution
unlike mice, humans and other primates have a second variant of glycogenin called glycogenin-2, which is mainly expressed in the liver
evolution
unlike mice, humans and other primates have a second variant of glycogenin called glycogenin-2, which is mainly expressed in the liver
malfunction
-
glycogen depletion in skeletal muscle is a result of a non-functional glycogenin-1 due to a Thr83Met substitution in glycogenin-1
malfunction
the glycogenin-1 mutation T82M causes glycogenosis. Substitution of Thr82 for serine but not for valine restores the maximum extent of autoglucosylation as well as transglucosylation and UDP-glucose hydrolysis rate, structure analysis, overview
malfunction
the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive
malfunction
analysis of GYG2 deletion phenotype and effects on glucose metabolism and/or glycogen synthesis, GYG2 deletion mutant phenotype overview, liver histopathology and enzyme expression level, overview
malfunction
glycogenin-2 is unable to glucosylate inactive glycogenin-1, at least not an enzymatically inactivated Thr83Met glycogenin-1 mutant, recently identified in a patient with severe glycogen depletion
malfunction
complete lack of glycogenin-1 is usually associated with late onset muscle weakness, indicating that lack of glycogenin-1 has no major impact on muscle energy metabolism. The muscle weakness that appears later in life is associated with muscle fiber degeneration, replacement of muscle tissue by fat and fibrous connective tissue explains the weakness. Several recessive pathogenic mutations have been identified in the glycogenin-1 gene, GYG1. Complete absence of glycogenin-1 protein secondary tobi-allelic truncating mutations in GYG1 causes a rare muscle disease that is characterized by accumulation of glycogen. This glycogen is, in addition to lack of a glycogenin-1 core, abnormal with regard to its ultrastructure. Many glycogen particles show uneven size and irregular shape, and some of the storage material has a fibrillar structure. A more severe heart disease associated with missense GYG1 mutations has been described in several individuals. Muscle glycogen depletion caused by truncating mutations in GYS1, which encodes the ubiquitously expressed glycogen synthase, does not result in a compensatory upregulation of the liver glycogen synthase isoform. In patients with total lack of glycogen due to muscle glycogen synthase deficiency, glycogenin-1 is present in similar quantities as in normal individuals
malfunction
etiology and pathogenesis of a late-onset myopathy associated with glycogenin-1 deficiency, overview. Two siblings heterozygous for two mutations in the glycogenin-1 gene, one 1-base deletion and one missense mutation, are analyzed. They show remarkably different clinical expression of the disease. There is no clear correlation between the genotype and the phenotypic expression even within the same family. Glycogenin-1 deficiency should be considered as a differential diagnosis in middle-aged and elderly individuals with slowly progressive myopathy, and it may present with highly variable distribution of weakness and wasting. Phenotypes, detailed overview
malfunction
glycogen storage disease (GSD) type XV is a rare disease caused by mutations in the GYG1 gene that codes for the core molecule of muscle glycogen, glycogenin 1. Nonetheless, glycogen is present in muscles of glycogenin 1-deficient patients due to activity of glycogenin 2. Apart from occurrence of polyglucosan (PG) bodies in few fibers, glycogen appears normal in most cells, and the concentration is normal in patients with GSD type XV. Analysis of formation of glycogen and changes in glycogen metabolism in patients with GSD type XV, overview
malfunction
glycogenin inactivation in mice results in an increased amount of glycogen and not glycogen depletion. Overproduction of glycogen secondary to glycogenin deficiency is associated with altered metabolism, affecting mainly oxidative muscle fibers and causing impaired endurance. Glycogenin KO mice show accumulation of glycogen instead of glycogen depletion, and no protein that functions as a substitute for glycogenin has been identified. The lack of glycogenin is associated with reduced endurance and a metabolic shift toward glycolytic metabolism in the otherwise fatigue-resistant oxidative muscle fibers. The results from the mouse glycogenin KO experiments support the concept that glycogenin is not mandatory for glycogen synthesis, although deficiency causes metabolic impairment with reduced endurance
malfunction
muscle glycogen depletion caused by truncating mutations in GYS1, which encodes the ubiquitously expressed glycogen synthase, does not result in a compensatory upregulation of the liver glycogen synthase isoform
physiological function
-
glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
physiological function
Asp162 is the residue involved in the activation step of the glucose transfer reaction mechanism
physiological function
glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis
physiological function
-
glycogenin-1 initiates the glycogen synthesis in skeletal muscle by the autocatalytic formation of a short oligosaccharide at tyrosine 195
physiological function
glycogen synthesis is initiated by self-glucosylation of the glycosyltransferases glycogenin-1 and -2 that, in the presence of UDP-glucose, form both the first glucose-O-tyrosine linkage, and then stepwise add a series of alpha1,4-linked glucoses to a growing chain of variable length. The self-glucosylation endpoint is only 0-4 glucose units on Tyr228 of glycogenin-2. The glucosylation of glycogenin-2 is enhanced to 2-4 glucose units by the presence of enzymatically active glycogenin-1
physiological function
glycogen synthesis is initiated by self-glucosylation of the glycosyltransferases glycogenin-1 and -2 that, in the presence of UDP-glucose, form both the first glucose-O-tyrosine linkage, and then stepwise add a series of alpha1,4-linked glucoses to a growing chain of variable length. The self-glucosylation endpoint is the incorporation of 4-8 glucose units on Tyr195 of glycogenin-1
physiological function
glycogenin-1 is a constitutively active enzyme so does not represent a point of regulation
physiological function
glycogenin-2 is dispensable for liver glycogen synthesis and glucagon-stimulated glucose release. Glycogenin-2 is not required for liver glycogen synthesis and glucagon-stimulated glucose release
physiological function
enzyme glycogenin 2 compensates for glycogenin 1 in human skeletal muscles of GYG1-deficient mutants. No expression of GYG2 occurs in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
physiological function
glycogenin 1 protein forms the core of glycogen in skeletal and cardiac muscle
physiological function
glycogenin is a core protein in glycogen particles and functions as a glycosyl transferase with the ability to autoglucosylate
physiological function
glycogenin is a core protein in glycogen particles and functions as a glycosyl transferase with the ability to autoglucosylate. A primer protein is dispensable for glycogen synthesis. Glycogenin appears to have a role in the regulation of glycogen content
physiological function
high glycogen levels in the Pacific oyster (Crassostrea gigas) contribute to its flavor, quality, and hardiness. Glycogenin (CgGN) is the priming glucosyltransferase that initiates glycogen biosynthesis. mRNA expression is closely related to glycogen content and CgGS expression
additional information
-
aggregation might be an explanation for the incomplete autoglucosylation of wild-type glycogenin-1
additional information
hGYG1 ccurs in two distinct states, the ground state and the active state, the two states are interchangeable during catalysis and involve conformational rearrangements in three regions that influence active site accessibility, overview
additional information
-
hGYG1 ccurs in two distinct states, the ground state and the active state, the two states are interchangeable during catalysis and involve conformational rearrangements in three regions that influence active site accessibility, overview
additional information
-
interaction and binding of wild-type full-length enzyme and truncated mutant CeGN34 to glycogen synthase, the CeGS-CeGN34 interaction is required for glycogen formation, overview
additional information
the recombinant glycogen synthase-glycogenin-1 complex GYS1:GN1 is functional and exhibits both allosteric and phospho-dependent regulatio, activation of GYS1:GN1 complex by GYS1 dephosphorylationn
additional information
-
the recombinant glycogen synthase-glycogenin-1 complex GYS1:GN1 is functional and exhibits both allosteric and phospho-dependent regulatio, activation of GYS1:GN1 complex by GYS1 dephosphorylationn
additional information
muscle glycogenin contains a single tyrosine, Tyr194, in covalent linkage with the first sugar unit, glucose, beta-phenyl-D-glucopyranoside (beta-PhGlc), confirming that tyrosine is fundamental for glycogen formation. Analysis of the mechanism for the early stages of the biosynthesis of glycogen. This macromolecule structure (PDB ID 3U2U) is constructed via the covalent attachment of glucose units to glycogenin, which remains covalently bonded to Tyr194 in a mature glycogen molecule. Isolation of the Tyr194 side chain in covalent linkage with glucose, of beta-phenyl-D-glucopyranoside, and examined the influence that the substitution of the tyrosine with different interacting reactants has on the preferred interaction sites, preferred interaction site for both alpha- and beta-Glc at body temperature is the 4-OH group of beta-PhGl, overview. The phenolic substituent of tyrosine is ideal, as it provides a rigid structure, acting as a hook for glucose, and the aromatic ring provides a tantalizing interacting environment that most molecules find entropically more favourable. The ability of glycogenin to elongate its glucan chain may reflect structural constraints both in the amino acid and at the catalytic site
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GLG1_YEAS7
Saccharomyces cerevisiae (strain YJM789)
616
0
69830
Swiss-Prot
Secretory Pathway (Reliability: 4)
GLG1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
616
0
69724
Swiss-Prot
Secretory Pathway (Reliability: 4)
GLG2_YEAS7
Saccharomyces cerevisiae (strain YJM789)
380
0
44577
Swiss-Prot
other Location (Reliability: 4)
GLG2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
380
0
44546
Swiss-Prot
other Location (Reliability: 4)
GLYG2_HUMAN
501
0
55184
Swiss-Prot
other Location (Reliability: 2)
GYG1_CAEEL
429
0
49007
Swiss-Prot
other Location (Reliability: 3)
GLYG_HUMAN
350
0
39384
Swiss-Prot
other Location (Reliability: 4)
GLYG_MOUSE
333
0
37402
Swiss-Prot
other Location (Reliability: 4)
GLYG_RABIT
333
0
37397
Swiss-Prot
other Location (Reliability: 4)
GLYG_RAT
333
0
37378
Swiss-Prot
other Location (Reliability: 4)
Q6DFG8_XENLA
332
0
37537
TrEMBL
other Location (Reliability: 2)
B9SIU1_RICCO
260
0
29459
TrEMBL
other Location (Reliability: 1)
A0A8B6HP07_MYTGA
262
0
29191
TrEMBL
other Location (Reliability: 3)
A0A171A0Y1_TRIIF
176
0
19593
TrEMBL
Mitochondrion (Reliability: 4)
A0A0B4K7X5_DROME
545
0
61748
TrEMBL
Mitochondrion (Reliability: 4)
B6KAA8_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
345
0
38717
TrEMBL
other Location (Reliability: 2)
B7PDN1_IXOSC
345
0
38714
TrEMBL
other Location (Reliability: 3)
A0A8J8WHM9_9EURO
739
0
82660
TrEMBL
other Location (Reliability: 4)
A0A1L3LQQ2_9HYPH
292
0
33084
TrEMBL
-
A0A8B6FJH9_MYTGA
202
0
22810
TrEMBL
other Location (Reliability: 1)
A0A086LGQ7_TOXGO
345
0
38717
TrEMBL
other Location (Reliability: 2)
E1JGQ3_DROME
287
0
32839
TrEMBL
other Location (Reliability: 1)
A0A139Y7Y6_TOXGO
345
0
38731
TrEMBL
other Location (Reliability: 2)
A0A7R8H8R2_LEPSM
395
0
44349
TrEMBL
other Location (Reliability: 1)
Q9W2J6_DROME
333
0
37776
TrEMBL
Mitochondrion (Reliability: 4)
A0A1V0PQI3_9RHOB
252
0
28690
TrEMBL
-
A0A2G9GXV4_9LAMI
179
0
21510
TrEMBL
other Location (Reliability: 3)
A0A8J5BE01_9ASCO
537
0
59670
TrEMBL
other Location (Reliability: 3)
A0A017HV07_9RHOB
265
0
29862
TrEMBL
-
E3TDQ3_ICTPU
323
0
36754
TrEMBL
other Location (Reliability: 3)
B9RFU2_RICCO
351
0
39058
TrEMBL
other Location (Reliability: 3)
A0A086KJF4_TOXGO
345
0
38717
TrEMBL
other Location (Reliability: 2)
A0A086PPS7_TOXGO
345
0
38645
TrEMBL
other Location (Reliability: 2)
A0A086QZS4_TOXGO
345
0
38663
TrEMBL
other Location (Reliability: 2)
A0A5B7BW33_DAVIN
474
5
53951
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0F8B4U9_CERFI
616
0
68624
TrEMBL
other Location (Reliability: 3)
A2RAV0_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
767
0
86570
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0B2SII6_GLYSO
503
0
58894
TrEMBL
Mitochondrion (Reliability: 5)
A0A2I0AZW4_9ASPA
473
6
53853
TrEMBL
other Location (Reliability: 5)
A0A2T6J2T9_TOXGO
345
0
38717
TrEMBL
other Location (Reliability: 2)
A0A7R8H7U4_LEPSM
359
0
40574
TrEMBL
other Location (Reliability: 1)
A3LQ29_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
411
0
46218
TrEMBL
other Location (Reliability: 3)
A0A0B4LFW5_DROME
699
0
78062
TrEMBL
Mitochondrion (Reliability: 4)
A0A1L3L6P8_9HYPH
269
0
30836
TrEMBL
-
A0A396HSQ1_MEDTR
485
5
55574
TrEMBL
Secretory Pathway (Reliability: 4)
Q5M7A1_XENTR
395
0
45103
TrEMBL
other Location (Reliability: 2)
B7PQ52_IXOSC
342
0
38723
TrEMBL
other Location (Reliability: 1)
B7PN36_IXOSC
258
0
29553
TrEMBL
other Location (Reliability: 1)
K0KTZ5_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
609
0
71585
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086MA85_TOXGO
345
0
38717
TrEMBL
other Location (Reliability: 2)
A0A812CA09_SEPPH
333
0
37846
TrEMBL
other Location (Reliability: 1)
G7JIW7_MEDTR
472
7
54098
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B4LG72_DROME
334
0
38053
TrEMBL
Mitochondrion (Reliability: 4)
A0A0B4LG29_DROME
356
0
40075
TrEMBL
Mitochondrion (Reliability: 4)
S7W1B4_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
345
0
38569
TrEMBL
other Location (Reliability: 2)
A0A8J5B534_9ASCO
523
0
57573
TrEMBL
other Location (Reliability: 4)
A0A8J5BH67_9ASCO
349
0
39938
TrEMBL
Secretory Pathway (Reliability: 1)
Q6DE98_XENLA
330
0
37384
TrEMBL
other Location (Reliability: 3)
Q9AV15_ORYSJ
492
6
56030
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6P8D4_ROSCH
463
5
52768
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8M1NTA8_DANRE
409
0
46225
TrEMBL
other Location (Reliability: 3)
A0A2G9GD05_9LAMI
175
5
19708
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5P9QE26_9MICO
657
0
71217
TrEMBL
-
A0A8J5CK09_9ASCO
351
0
39928
TrEMBL
Secretory Pathway (Reliability: 2)
A3GFI3_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
625
0
70911
TrEMBL
other Location (Reliability: 3)
A0A151SKN6_CAJCA
470
6
53287
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G8XT48_TOXGO
345
0
38717
TrEMBL
other Location (Reliability: 2)
A0A0B3RMC0_9RHOB
264
0
29645
TrEMBL
-
A0A3R8ARN1_TOXGO
345
0
38731
TrEMBL
other Location (Reliability: 2)
A0A017H8E9_9RHOB
277
0
31092
TrEMBL
-
A0A0B2SBD8_GLYSO
477
6
54254
TrEMBL
Secretory Pathway (Reliability: 3)
B9S7N5_RICCO
776
5
87774
TrEMBL
other Location (Reliability: 2)
W6RDZ6_9HYPH
276
0
31825
TrEMBL
-
A0A0B2RDP3_GLYSO
551
6
61617
TrEMBL
Secretory Pathway (Reliability: 1)
A8E607_XENLA
362
0
41247
TrEMBL
other Location (Reliability: 2)
K0KTS0_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
344
0
39607
TrEMBL
other Location (Reliability: 3)
A0A2G9GD02_9LAMI
465
6
53167
TrEMBL
Mitochondrion (Reliability: 4)
A0A2G9H765_9LAMI
467
5
53387
TrEMBL
Mitochondrion (Reliability: 5)
Q7APB7_RHIME
Rhizobium meliloti (strain 1021)
291
0
33143
TrEMBL
-
A2QXX9_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
320
0
36044
TrEMBL
other Location (Reliability: 3)
Q803Q1_DANRE
329
0
36995
TrEMBL
other Location (Reliability: 2)
A0A5B7AY84_DAVIN
321
5
36050
TrEMBL
other Location (Reliability: 4)
A0A2I0AVK3_9ASPA
478
5
54201
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2I0AI21_9ASPA
732
0
84783
TrEMBL
other Location (Reliability: 3)
A0A086K943_TOXGO
345
0
38645
TrEMBL
other Location (Reliability: 2)
A0A6J8AKX1_MYTCO
812
0
88634
TrEMBL
other Location (Reliability: 1)
Q6P328_XENTR
332
0
37379
TrEMBL
other Location (Reliability: 3)
A0A125YHG0_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
345
0
38717
TrEMBL
other Location (Reliability: 2)
K1R9A7_CRAGI
539
0
59834
TrEMBL
-
Q6Q2C8_NEUCS
664
0
73252
TrEMBL
other Location (Reliability: 2)
Q75PR2_ORYSI
379
0
43587
TrEMBL
Chloroplast (Reliability: 3)
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Y194F
-
site-directed mutagenesis, inactive mutant
D56H/D160T
naturally occuring mutations c.166G.C (p.Asp56His)/c.472Del (p.Asp160Thr fs*5) in GYG1 causing glycogen storage disease (GSD) type XV, phenotype, overview
G135R
determination of a naturally occuring missense mutation that causes reduced expression of glycogenin-1 protein and abolishes the enzyme's activity and function, phenotype includes altered morphology, muscle weakness and wasting, overview
T83A
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83C
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83F
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83S
-
site-directed mutagenesis, the mutant is catalytically active
T83V
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83Y
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
Y195F
-
site-directed mutagenesis, glycogenin-1 with the Thr83Met substitution is unable to form the glucose-O-tyrosine linkage at tyrosine 195 unless co-expressed with the catalytically active Tyr195Phe glycogenin-1
DELTA306-664
7fold increase in self-glucosylation
DELTA306-664/Y196F
no self-glucosylation activity
DELTA306-664/Y196F/Y198F
expression results in no accumulation of glycogen
DELTA360-664
11.8fold increase in self-glucosylation
DELTA360-664/Y196F
expression results in reduced glycogen accumulation to 30% of the wild-type enzyme, very low self-glucosylation activity
DELTA360-664/Y196F/Y198F
no self-glucosylation activity
D159N
exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer, self-glucosylation activities below the limit of detection of the assay. Ability to catalyze the transglucosylation of maltose is reduced by 260fold, hydrolysis of UDP-glucose is reduced 12fold
D159S
stable enzyme, self-glucosylation activities below the limit of detection of the assay. Transglucosylation activity of the mutant enzyme is reduced to undetectable levels, activity for the hydrolysis of UDP-glucose is reduced 14fold
D162N
exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer, self-glucosylation activities below the limit of detection of the assay, undetectable activity for the transglucosylation of maltose and the hydrolysis of UDP-glucose to free glucose
D162S
stable enzyme, self-glucosylation activities below the limit of detection of the assay. 30fold less active for the trans-glucosylation of maltose and 340fold less active for the hydrolysis of UDP-glucose
DELTA270-332
mutant enzyme is fully active, specific activity for self- or transglucosylation is indistinguishable from the full-length enzyme
DELTA270-332/D159S
inactive mutant enzyme
DELTA270-332/D162N
exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer
DELTA270-332/D162S
18fold less active for the transglucosylation of maltose and 190fold less active for the hydrolysis of UDP-glucose than wild-type enzyme, activity for the hydrolysis of UDP-glucose is reduced 4fold
T82M
inactive mutant, the mutation is equivalent to T83M according to previous authors amino acid numbering, it causes glycogenosis showing the loss of Thr82 hydrogen bond to Asp162, the residue involved in the activation step of the glucose transfer reaction mechanism. Autoglucosylation, maltoside transglucosylation and UDP-glucose hydrolyzing activities are abolished
T83S
site-directed mutagenesis, the mutant is catalytically active
T83V
site-directed mutagenesis, inactive mutant
Y194F
-
exchange of glucose attachment site, no autoglucosylation activity
Y194X
-
mutation at Y194 leads to a protein unable to attach glucose to itself
Y194T
-
exchange of glucose attachment site, no autoglucosylation activity, mutant glycosylates other substrates but with less activity compared to the wild-type
D163T
a naturall yoccuring truncating 1-base deletion (c.484delG; p.Asp163Thrfs*5) causes reduced expression of glycogenin-1 protein, the phenotype includes altered morphology, muscle weakness and wasting, overview
D163T
naturally occuring mutation c.487del (p.Asp163Thrfs*5) in GYG1 causing glycogen storage disease (GSD) type XV, phenotype, overview
T83M
-
naturally occuring mutation, glycogenin-1 with the Thr83Met substitution is unable to form the glucose-O-tyrosine linkage at tyrosine 195 unless co-expressed with the catalytically active Tyr195Phe glycogenin-1. The mutant shows no incorporation of glucose, no autoglycosylation
T83M
the Thr83Met mutant is structurally ablated in forming the active state, molecular basis, the mutation is linked with glycogen storage disease XV, GSD type XV. hGYG1T83M is not endogenously glucosylated
T83M
naturally occuring mutation of glycogenin-1, earlier detected in a patient with glycogen depletion in the skeletal muscle, the mutated glycogenin-1 is catalytically inactive and unable to become self-glucosylated or glycosylated by wild-type glycogenin-2, but it can be glucosylated by the catalytically active Y195F glycogenin-1 mutant
Y194F
-
mutant glycosylates other substrates with nearly the same activity as the wild-type
Y194F
-
exchange of glucose attachment site, no autoglucosylation activity
additional information
-
-
deletion construct pGEX-GN (263-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
additional information
-
-
deletion construct pGEX-GN (297-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
additional information
-
-
deletion construct pGEX-GN (301-333). The fragment of glycogenin is fused with glutathione-S-transferase (GST). The fusion protein is able to precipitate glycogen synthase in the presence of glutathione-agarose.
additional information
-
construction of a truncated enzyme version CeGN34. The CeGNDELTAC mutant is defective for interaction with glycogen synthase CeGS
additional information
-
non-glucosylated glycogenin-1 constructs, with various amino acid substitutions in position 83 and 195, are expressed in a cell-free expression system and autoglucosylated in vitro
additional information
-
expression analysis of GYG2 in wild-type and GYG1-deficient mutant muscle tissue samples, no expression of GYG2 in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
additional information
expression analysis of GYG2 in wild-type and GYG1-deficient mutant muscle tissue samples, no expression of GYG2 in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
additional information
-
two patients with mutations in the GYG1 gene are investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism, phenotypes, overview
additional information
two patients with mutations in the GYG1 gene are investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism, phenotypes, overview
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