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Information on EC 2.4.1.186 - glycogenin glucosyltransferase and Organism(s) Homo sapiens and UniProt Accession P46976

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.186 glycogenin glucosyltransferase
IUBMB Comments
The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme's Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains . It continues to glucosylate an existing glucosyl group until a length of about 5--13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
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Homo sapiens
UNIPROT: P46976
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
glycogenin, glycogenin-1, glycogenin-2, priming glucosyltransferase, m-glycogenin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycogenin
glycogenin-1
glycogenin-2
glyogenin
-
-
-
-
GN-1
285776
-
GN1
285776
-
GN2
304467
-
GYG
247
-
hGYG1
285776
-
priming glucosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
conformational plasticity of glycogenin and coexistence of two modes of glucosylation as integral to its catalytic mechanism, possible SNi-like mechanism for glucosyl-transfer, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:glycogenin alpha-D-glucosyltransferase
The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme's Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains [7]. It continues to glucosylate an existing glucosyl group until a length of about 5--13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
CAS REGISTRY NUMBER
COMMENTARY hide
117590-73-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
show the reaction diagram
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
show the reaction diagram
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
-
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
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
show the reaction diagram
O15488
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
P46976
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
show the reaction diagram
O15488
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
Mn2+
-
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from breast tissue
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive
physiological function
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
GLYG_HUMAN
350
0
39384
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
recombinant His-tagged unglucosylated glycogenin-1, gel filtration
41000
-
recombinant His-tagged autoglucosylated glycogenin-1, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the degree of glycosylation of the enzyme is modest
glycoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
purified recombinant hGYG1 in complex with Mn2+ and UDP-alpha-glucose, 10 mg/ml hGYG1 with various ligands by sitting drop vapor diffusion at 20°C, X-ray diffraction structure determination and analysis at 2.6 A, molecular replacement
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
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
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged glycogen synthase in complex with glycogenin-1 from Sf9 insect cells by glutathione affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chrmatography
-
recombinant His6-tagged wild-type and mutant glycogenin-1 from HEK-293 cells by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from cell-free expression by nickel affinity chromatography
-
recombinant His6-tagged wild-type and mutant glycogenin-2 from HEK-293 cells by nickel affinity chromatography
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene GYG1, recombinant expression of functional GST-tagged human muscle glycogen synthase in complex with human glycogenin-1 in Spodoptera frugiperda Sf9 cells using a bicistronic pFastBac™-Dual expression vector and baculovirus transfection
recombinant expression of His6-tagged wild-type and mutant enzymes glycogenin-1 in HEK-293 cells. Coexpression of wild-type glycogenin-2 together with different glycogenin-1 variants using a cell-free system, coexpression of functional glycogenin-1 and glycogenin-2 increases the glucosylation of glycogenin-2
cell-free expression of His-tagged wild-type and mutant enzymes
-
expressed in C2C12 cells
-
gene GYG2, genotyping
recombinant expression of His6-tagged wild-type and mutant glycogenin-2 in HEK-293 cells. Coexpression of wild-type glycogenin-2 together with different glycogenin-1 variants using a cell-free system, coexpression of functional glycogenin-1 and glycogenin-2 increases the glucosylation of glycogenin-2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shearer, J.; Wilson, R.J.; Battram, D.S.; Richter, E.A.; Robinson, D.L.; Bakovic, M.; Graham, T.E.
Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle
Am. J. Physiol.
289
E508-514
2005
Homo sapiens
Manually annotated by BRENDA team
Barbetti, F.; Rocchi, M.; Bossolasco, R.; et a.
The human skeletal muscle glycogenin gene: cDNA, tissue expression and chromosomal localization
Biochem. Biophys. Res. Commun.
220
72-77
1996
Homo sapiens, Homo sapiens (P46976)
Manually annotated by BRENDA team
van Maanen, M.H.; Fournier, P.A.; Palmer, T.N.; Abraham, L.J.
Characterization of the human glycogenin-1 gene: identification of a muscle-specific regulatory domain
Gene
234
217-226
1999
Homo sapiens
Manually annotated by BRENDA team
Zhai, L.; Mu, J.; Zong, H.; DePaoli-Roach, A.A.; Roach, P.J.
Structure and chromosomal localization of the human glycogenin-2 gene GYG2
Gene
242
229-235
2000
Homo sapiens, Homo sapiens (P46976)
Manually annotated by BRENDA team
Skurat, A.V.; Dietrich, A.D.; Roach, P.J.
Interaction between glycogenin and glycogen synthase
Arch. Biochem. Biophys.
456
93-97
2006
Homo sapiens
Manually annotated by BRENDA team
Wilson, R.J.; Gusba, J.E.; Robinson, D.L.; Graham, T.E.
Glycogenin protein and mRNA expression in response to changing glycogen concentration in exercise and recovery
Am. J. Physiol.
292
E1815-E1822
2007
Homo sapiens (P46976)
Manually annotated by BRENDA team
Douillard-Guilloux, G.; Raben, N.; Takikita, S.; Batista, L.; Caillaud, C.; Richard, E.
Modulation of glycogen synthesis by RNA interference: Towards a new therapeutic approach for glycogenosis type II
Hum. Mol. Genet.
17
3876-3886
2008
Homo sapiens
Manually annotated by BRENDA team
Nilsson, J.; Halim, A.; Moslemi, A.R.; Pedersen, A.; Nilsson, J.; Larson, G.; Oldfors, A.
Molecular pathogenesis of a new glycogenosis caused by a glycogenin-1 mutation
Biochim. Biophys. Acta
1822
493-499
2012
Homo sapiens
Manually annotated by BRENDA team
Chaikuad, A.; Froese, D.; Berridge, G.; Von Delft, F.; Oppermann, U.; Yue, W.
Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis
Proc. Natl. Acad. Sci. USA
108
21028-21033
2011
Homo sapiens, Homo sapiens (P46976)
Manually annotated by BRENDA team
Nilsson, J.; Halim, A.; Larsson, E.; Moslemi, A.R.; Oldfors, A.; Larson, G.; Nilsson, J.
LC-MS/MS characterization of combined glycogenin-1 and glycogenin-2 enzymatic activities reveals their self-glucosylation preferences
Biochim. Biophys. Acta
1844
398-405
2014
Homo sapiens (O15488), Homo sapiens (P46976)
Manually annotated by BRENDA team
Irgens, H.U.; Fjeld, K.; Johansson, B.B.; Ringdal, M.; Immervoll, H.; Leh, S.; Sovik, O.; Johansson, S.; Molven, A.; Njolstad, P.R.
Glycogenin-2 is dispensable for liver glycogen synthesis and glucagon-stimulated glucose release
J. Clin. Endocrinol. Metab.
100
E767-E775
2015
Homo sapiens, Homo sapiens (O15488)
Manually annotated by BRENDA team
Hunter, R.W.; Zeqiraj, E.; Morrice, N.; Sicheri, F.; Sakamoto, K.
Expression and purification of functional human glycogen synthase-1:glycogenin-1 complex in insect cells
Protein Expr. Purif.
108
23-29
2015
Homo sapiens, Homo sapiens (P46976)
Manually annotated by BRENDA team
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