2.4.1.186: glycogenin glucosyltransferase
This is an abbreviated version!
For detailed information about glycogenin glucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.186
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2.4.1.186
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self-glucosylating
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glucosylation
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autoglucosylation
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polyglucosan
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proteoglycogen
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macroglycogen
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maltosaccharide
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transglucosylation
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analysis
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synthesis
- 2.4.1.186
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self-glucosylating
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glucosylation
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autoglucosylation
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polyglucosan
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proteoglycogen
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macroglycogen
- maltosaccharide
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transglucosylation
- analysis
- synthesis
Reaction
Synonyms
CeGN, CgGN, CgGN-alpha, CgGN-beta, CgGN-gamma, EC 2.4.1.112, glucosyltransferase, uridine diphosphoglucose-protein, glucosyltransferase, uridine diphosphoglucose-protein 4-alpha-, glycogen initiator synthase, glycogenin, glycogenin 1, glycogenin 2, glycogenin glycosyltransferase, glycogenin-1, glycogenin-2, glyogenin, GN-1, GN1, GN2, GNN, GYG, GYG1, GYG2, hGYG1, M-glycogenin, priming glucosyltransferase, proglycogen synthase, UDP-glucose protein transglucosylase, UDP-glucose-protein glucosyltransferase, UDP-glucose:protein glucosyltransferase, UDPGlc:protein transglucosylase, UPTG, uridine diphosphate glucose-protein transglucosylase I, uridine diphosphoglucose protein transglucosylase I, uridine diphosphoglucose-protein 4-alpha-glucosyltransferase, uridine diphosphoglucose-protein glucosyltransferase
ECTree
2.4.1.186 glycogenin glucosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.186 - glycogenin glucosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D163T
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
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site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83C
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site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83F
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site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83M
T83V
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site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83Y
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site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
Y195F
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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/Y196F/Y198F
expression results in no accumulation of glycogen
DELTA360-664/Y196F
expression results in reduced glycogen accumulation to 30% of the wild-type enzyme, very low 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/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
Y194F
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exchange of glucose attachment site, no autoglucosylation activity
Y194X
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mutation at Y194 leads to a protein unable to attach glucose to itself
Y194F
Y194T
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exchange of glucose attachment site, no autoglucosylation activity, mutant glycosylates other substrates but with less activity compared to the wild-type
additional information
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
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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
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mutant glycosylates other substrates with nearly the same activity as the wild-type
Y194F
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exchange of glucose attachment site, no autoglucosylation activity
additional information
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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
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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
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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
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construction of a truncated enzyme version CeGN34. The CeGNDELTAC mutant is defective for interaction with glycogen synthase CeGS
additional information
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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
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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
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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
