Information on EC 2.4.1.186 - glycogenin glucosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.4.1.186
-
RECOMMENDED NAME
GeneOntology No.
glycogenin glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
The glycogenin subunit of glycogen synthase (EC 2.4.1.11, glycogen(starch) synthase) catalyses this reaction, i.e. the enzyme catalyses its own autoglycosylation. Five molecules of glucose can be transferred to one molecule of glycogenin. The product acts as a primer for the reaction catalysed by glycogen synthase.
-
-
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein; stereochemistry and mechanism
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein; independent active sites for glucosylation of exogenous and self-acceptors
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein; initiation of glycogen biosynthesis is a 2-step mechanism, requiring first the covalent attachment of a glucose residue to Tyr-194 of glycogenin and then elongation to form an oligosaccharide chain
-
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
show the reaction diagram
highly conserved protein
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glycogen biosynthesis II (from UDP-D-Glucose)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycogenin
-
-
-
glycogenin
-
-
glycogenin
P46976
-
glycogenin
-
-
glycogenin
P13280
-
glycogenin
-
-
glycogenin glycosyltransferase
-
-
glycogenin-1
-
-
glycogenin-1
P46976
-
glycogenin-1
P13280
-
glycogenin-2
-
-
glyogenin
-
-
-
-
GN-1
P46976
-
GNN
Q6Q2C8
-
hGYG1
P46976
-
priming glucosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
117590-73-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Coturnix sp.
Quail
-
-
Manually annotated by BRENDA team
recreationally active males, only slight decrease of enzyme level upon exercise with fast restoring of initial level upon recreation
UniProt
Manually annotated by BRENDA team
the amino acid residues 301-333 in glycogenin are engaged in interaction with glycogen synthase. Glycogenin contains at least one additional interacting site for glycogen synthase beside the COOH-terminus.
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Hampshire crossbred animals with and without presence of th RN- allele. The total muscle glucose content 0.5 h post-mortem is 77% higher in RN- carriers compared with wild type animals. A greater transcription of glycogenin is found in RN- carriers. The glycogenin m-RNA is more abundant in RN- carriers compared with wild type animals.
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
physiological function
-
glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
physiological function
-
glycogenin-1 initiates the glycogen synthesis in skeletal muscle by the autocatalytic formation of a short oligosaccharide at tyrosine 195
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
malfunction
-
the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-glucose + glycogenin
CDP + glucosylated glycogenin
show the reaction diagram
-
recombinant enzyme expressed in E. coli, 71% activity compared to UDP-glucose
-
?
TDP-glucose + glycogenin
TDP + glucosylated glycogenin
show the reaction diagram
-
recombinant enzyme expressed in E. coli, 33% activity compared to UDP-glucose
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-galactose + glycogenin
UDP + galactosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
glucose molecule is attached to Tyr-194
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
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
show the reaction diagram
-
one attached glucose molecule is needed for intramolecular self-glucosylation
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
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
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
no activity with UDP-N-acetylglucosamine and GDP-mannose
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
no activity with CDP-glucose, UDP-glucose can not be replaced by ADP- or GDP-glucose
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
UDP-glucose can not be replaced by ADP- or GDP-glucose
forms glucosyl-alpha1,4-glucosyl linkage
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
regulation
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
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
show the reaction diagram
-
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
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-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 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
show the reaction diagram
-
autoglucosylation
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
Q6Q2C8
-
-
-
?
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
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
Q6Q2C8
self-glucosylating initiator of glycogen synthesis
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
P13280
self-glucosylation
-
-
?
UDP-glucose + maltose
UDP + maltotriose
show the reaction diagram
P13280
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
show the reaction diagram
-
simultaneously and independently of the autoglycosylation reaction, peptide sequence: SISIYSYLP
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
-
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
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
show the reaction diagram
-
renal enzyme
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
transglucosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
transglucosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
transglucosylation reaction
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
simultaneously and independently of the autoglycosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
simultaneously and independently of the autoglycosylation reaction
-
-
?
UDP-glucose + n-dodecyl-beta-D-maltoside
UDP + n-dodecyl-beta-D-maltotriose
show the reaction diagram
-
simultaneously and independently of the autoglycosylation reaction
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
show the reaction diagram
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-alpha-D-maltoside
?
show the reaction diagram
-
transglucosylation reaction
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
show the reaction diagram
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-octyl-beta-D-maltoside
?
show the reaction diagram
-
transglucosylation reaction
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
show the reaction diagram
-
hydrophobic nature of the aglycon is required for binding to the active site
-
-
?
UDP-glucose + n-tetradecyl-beta-D-maltoside
?
show the reaction diagram
-
transglucosylation reaction
-
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
show the reaction diagram
-
autoglycosylation reaction
-
?
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
show the reaction diagram
-
renal and skeletal muscle glycogenin, lower activity compared to UDP-glucose
-
?
UDP-xylose + n-dodecyl-beta-D-maltoside
?
show the reaction diagram
-
transglucosylation reaction
-
-
?
CDP-glucose + p-nitrophenyl-alpha-maltoside
CDP + glucosylated p-nitrophenyl-alpha-maltoside
show the reaction diagram
-
recombinant enzyme expressed in E. coli
-
-
?
additional information
?
-
-
no activity with nonapeptide SISIYSYLP and N-lactosylated peptide
-
-
-
additional information
?
-
-, Q75PR2
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
?
-
-
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
-
-
-
TDP-glucose + p-nitrophenyl-alpha-maltoside
TDP + glucosylated p-nitrophenyl-alpha-maltoside
show the reaction diagram
-
recombinant enzyme expressed in E. coli
-
-
?
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
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
-
autoglucosylation by glycogenin-1
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
-
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
enzyme forms the protein part of proteoglycogen
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
regulation
-
-
-
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
-
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
show the reaction diagram
-
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
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-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 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 + 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
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
show the reaction diagram
Q6Q2C8
self-glucosylating initiator of glycogen synthesis
-
-
?
additional information
?
-
-, Q75PR2
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
less effective than Mn2+
Mg2+
-
can not substitute Mn2+
Mn2+
-
absolutely dependent on divalent cations, Mn2+ can be replaced by Mg2+ with less effectivity
Mn2+
-
dependent on, also required for transglucosylation
Mn2+
-
dependent on, also required for transglucosylation
Mn2+
-
enhances self-glucosylation activity and trans-glucosylation activity
Mn2+
-
required for activity
Mn2+
-
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
skeletal muscle enzyme, allosteric inhibition of autoglucosylation
ATP
-
skeletal muscle enzyme, allosteric inhibition of autoglucosylation, complete inhibition at 5 mM, possible role as natural regulator
ATP
-
slight inhibition, renal enzyme
CDP
-
renal enzyme, 90% inhibition at 0.025 mM
CDP-choline
-
renal enzyme, 75% inhibition at 0.1 mM
phosphate
-
slight inhibition at 100 mM
UDP
-
inhibits both autoglucosylation and glucosylation of exogenous acceptor
UDP
-
inhibits both autoglucosylation and glucosylation of exogenous acceptor
UDP-xylose
-
competitive inhibitor to glucosylation of glycogenin by UDP-glucose
maltose
-
very poor, 50% inhibition at 40 mM
additional information
-
no inhibition by phosphorylation of catalytic subunit of the glycogen synthase complex; not inhibitory: UDP-pyridoxal, LiBr
-
additional information
Coturnix sp.
-
enzyme is phosphorylated in embryonic muscle
-
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
Coturnix sp.
-
enzyme is phosphorylated in embryonic muscle
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
n-dodecyl-beta-D-maltoside
-
-
3
-
p-nitrophenyl-alpha-maltoside
-
-
0.002
-
UDP-glucose
-
-
0.00441
-
UDP-glucose
Q6Q2C8
-
additional information
-
additional information
-
Km-values for UDP-glucose in different tissues
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0053
-
UDP-glucose
-
glucosylated protein, 14C-glucose incorporation assay
0.0083
-
UDP-glucose
-
glucosylated protein, 4-10 interval, mass sprectrometry assay; non-glucosylated protein, 14C-glucose incorporation assay
0.0183
-
UDP-glucose
-
non-glucosylated protein, mass sprectrometry assay
additional information
-
additional information
-
the catalytic effectiveness of glycogenin falls off dramatically as the average glucosyl chain length increases
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
assay at
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Coturnix sp.
-
-
Manually annotated by BRENDA team
-
very low content
Manually annotated by BRENDA team
-
the samples for gene expression analyses are taken 0.5 h after slaughter
Manually annotated by BRENDA team
-
-
skeletal muscle library
Manually annotated by BRENDA team
Coturnix sp.
-
-
Manually annotated by BRENDA team
additional information
-
a glycogenin-like protein has also been found in retina
Manually annotated by BRENDA team
additional information
-
enzyme activity does not depend on physiological state of the organism
Manually annotated by BRENDA team
additional information
-
a glycogenin-like protein has also been found in thymus, brain, heart; enzyme activity does not depend on physiological state of the organism
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not membrane-bound
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
31000
-
-
SDS-PAGE
32000
-
-
kidney enzyme
34000
-
-
non-glycosylated truncated protein, gel filtration of a 0.0005 mM solution
37280
-
-
amino acid sequence determination
38000
-
-
gel filtration, SDS-PAGE, glycogenin glucosyltransferase represents the smaller subunit of glycogen synthase
38000
-
-
SDS-PAGE
40000
-
-
recombinant His-tagged unglucosylated glycogenin-1, gel filtration
41000
-
-
recombinant His-tagged autoglucosylated glycogenin-1, gel filtration
47000
-
-
a glycogenin species of average molecular weight 47000 Da is isolated from proteoglycogen isoamylolyzed for 4.5 h, SDS-PAGE
58000
-
-
truncation mutant enzymes DELTA270-332/D159S and DELTA270-332/D162S, gel filtration
59000
-
-
non-glycosylated truncated protein, gel filtration of a 0.02 mM solution
103000
-
-
wild-type enzyme in glycosylated and nonglycosylated form, full-length mutant enzymes D162S and D159S, gel filtration
124000
-
-
gel filtration, heterodimeric glycogen synthase complex
200000
-
-
gel filtration, active proteoglycogen
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 31000, SDS-PAGE
dimer
-
truncation mutant enzymes DELTA270-332/D159S and DELTA270/D162S, wild-type enzyme in glycosylated and nonglycosylated form, full-length mutant enzymes D162S and D159S exists as more than 95% dimer. Mutant enzymes D159N, D162N and DELTA270-332/D162N exist as both tetrameric and dimeric species
dimer
-
2 * 34000, non-glycosylated truncated protein, 0.02 mM enzyme solution; 2 * 38000, native enzyme
tetramer
-
mutant enzymes D159N, D162N and DELTA270-332/D162N exist as both tetrameric and dimeric species
monomer
-
1 * 34000, non-glycosylated truncated protein, 0.0005 mM enzyme solution; 1 * 38000, native enzyme, 50-70% of the activity of the dimer
additional information
-
glycogenin glucosyltransferase, MW 38 kDa, represents the smaller subunit of glycogen synthase, both enzyme form a heterodimeric complex of molar ratio 1:1
additional information
-
enzyme forms the protein part of proteoglycogen; in muscle a glycogen beta-particle is bound to glycogenin in a 1:1 ratio, the enzyme/glycogen ratio in liver is lower
additional information
-
enzyme forms the protein part of proteoglycogen; glycogenin glucosyltransferase, MW 38 kDa, represents the smaller subunit of glycogen synthase, both enzyme form a heterodimeric complex of molar ratio 1:1; in muscle a glycogen beta-particle is bound to glycogenin in a 1:1 ratio, the enzyme/glycogen ratio in liver is lower
additional information
-
glycogenin glucosyltransferase, MW 38 kDa, represents the smaller subunit of glycogen synthase, both enzyme form a heterodimeric complex of molar ratio 1:1; purified glycogenin associates as a dimer in absence of SDS, MW 64 kDa, glycerol density gradient centrifugation
additional information
-
enzyme forms the protein part of proteoglycogen
additional information
-
enzyme forms the protein part of proteoglycogen
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 ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
autoglycosylation
glycoprotein
-
autoglycosylation
glycoprotein
-
glycogenin is a self-glycosylating protein primer
glycoprotein
-
in vitro autoglucosylation of wild-type and mutant enzymes
glycoprotein
-
autoglycosylation
glycoprotein
-
autoglycosylation
glycoprotein
Q6Q2C8
two glucosylation sites Tyr196 and Tyr198. The enzyme is a self-glucosylating initiator of glycogen synthesis, recombinant enzyme contains an oligosaccharide chain attached to Tyr196
glycoprotein
-
autoglycosylation; five molecules of glucose can be transferred to one molecule of glycogenin, which contains already 1 glucose molecule prior to autoglycosylation
glycoprotein
-
1 single glucose attachment site at tyrosine-194; autoglycosylation
glycoprotein
-
self-glucosylated at Tyr194 and Tyr232
glycoprotein
-
-
glycoprotein
-
self-glucosylation. Asp162 is an intermediate nucleophilic acceptor in the active site of the enzyme from which the glucose is delivered directly to Tyr194 or to glucose residues already attached to Tyr194
glycoprotein
-
autoglycosylation
glycoprotein
-
autoglycosylation; one attached glucose molecule is needed for intramolecular self-glucosylation
glycoprotein
-
autoglycosylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 20C, X-ray diffraction structure determination and analysis at 2.6 A, molecular replacement
-
purified recombinant glycogenin-1 truncation mutant DELTA-270, hanging drop vapor diffusion method, the protein in 12% w/v, PEG monomethyl ester 5000, 0.1 M MES, pH 6.5, and 0.2 M ammonium sulfate, is mixed with 1 M ammonium sulfate and 0.1 M sodium phosphate, pH 6.7, 4C, crystals are soaked in mother liquor containing 1 mM MnSO4 and 1 mM UDP or UDP-glucose, X-ray diffraction structure determination and analysis
-
the DELTA270 enzyme crystallizes at 7.5 mg/ml from solutions containing 1 mM UDP-glucose, 1 mM MnCl2, 100 mM sodium acetate, pH 4.54.7, and 1013% (w/v) PEG 4000 in the space group P64, with cell dimensions a = b = 75.0, c = 233.4, gamma = 120 and a dimer in the asymmetric unit. All crystals are grown using hanging drop vapor diffusion methods at 23C
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity on Q-Sepharose during ion exchange chromatography
-
concentrated to 8 mg/ml, and 100 microl aliquots are flash frozen in liquid nitrogen and stored at -80C. Glycogenin stored in this manner is stable for at least 2 years.
-
alkali-stable
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, amylolyzed M-glycogenin preparation, at least 1 month without appreciable loss of activity
-
4C, amylolyzed M-glycogenin preparation, at least 1 week without appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from cell-free expression by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chrmatography
-
separation from proteoglycogen
-
Ni-Sepharose column chromatography and Q Sepharose column chromatography
-
nickel-NTA column and Q-Sepharose column
-
recombinant proteins
-
recombinant wild-type gycogenin-1, its truncated mutant DELTA-270, and of glycogenin-1 point mutants from Escherichia coli strain CGSC 4997
-
separation from glycogen synthase, EC 2.4.1.11, by LiBr
-
separation from proteoglycogen
-
wild-type and mutant enzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cell-free expression of His-tagged wild-type and mutant enzymes
-
expressed in C2C12 cells
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli as a GST-tagged protein
Q6Q2C8
isolation of cDNA
-
expressed in Escherichia coli strain Rosetta (DE3)
-
expression in COS cells; expression of mutant Y194F in Escherichia coli
-
expression of mutant Y194F in Escherichia coli; functional expression of the wild-type enzyme in Escherichia coli
-
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
expression of wild-type gycogenin-1, its truncated mutant DELTA-270, and of glycogenin-1 point mutants in Escherichia coli strain CGSC 4997
-
expresssion of recombinant protein in the CGSC Escherichia coli cell line 4997, which lacks UDP-glucose pyrophosphorylase activity
-
preparation of a truncated already glucosylated His-tag fusion protein in Escherichia coli ER2566, expression of the truncated non-glucosylated His-tag fusion protein in Escherichia coli CGSC 4997
-
-
-, Q75PR2
expression of glucose-free apo-glycogenin in an Escherichia coli mutant lacking UDP-glucose, enzyme is active towards itself and other substrates
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
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
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
Q6Q2C8
7fold increase in self-glucosylation
DELTA306-664/Y196F
Q6Q2C8
no self-glucosylation activity
DELTA306-664/Y196F/Y198F
Q6Q2C8
expression results in no accumulation of glycogen
DELTA360-664
Q6Q2C8
11.8fold increase in self-glucosylation
DELTA360-664/Y196F
Q6Q2C8
expression results in reduced glycogen accumulation to 30% of the wild-type enzyme, very low self-glucosylation activity
DELTA360-664/Y196F/Y198F
Q6Q2C8
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
Y194F
-
exchange of glucose attachment site, no autoglucosylation activity; mutant glycosylates other substrates with nearly the same activity as the wild-type
Y194F
-
exchange of glucose attachment site, no autoglucosylation activity
Y194T
-
exchange of glucose attachment site, no autoglucosylation activity, mutant glycosylates other substrates but with less activity compared to the wild-type
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.; 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.; 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
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
-
the COOH-terminal fragment of glycogenin can be used as a effective high affinity reagent for the purification of glycogen synthase from skeletal muscle and liver
analysis
-
development of assay method with n-dodecyl-beta-D-maltoside as substrate