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Information on EC 2.4.1.186 - glycogenin glucosyltransferase and Organism(s) Mus musculus

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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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Mus musculus
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glycogenin, glycogenin-1, glycogenin-2, priming glucosyltransferase, glycogenin 1, glycogenin 2, m-glycogenin, glycogenin glucosyltransferase, proglycogen synthase, udp-glucose protein transglucosylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucosyltransferase, uridine diphosphoglucose-protein
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glucosyltransferase, uridine diphosphoglucose-protein 4-alpha-
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glycogen initiator synthase
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glycogenin
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glycogenin-1
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glyogenin
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priming glucosyltransferase
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proglycogen synthase
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UDP-glucose protein transglucosylase
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UDP-glucose-protein glucosyltransferase
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UDP-glucose:protein glucosyltransferase
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UDPGlc:protein transglucosylase
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UPTG
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uridine diphosphate glucose-protein transglucosylase I
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uridine diphosphoglucose protein transglucosylase I
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uridine diphosphoglucose-protein 4-alpha-glucosyltransferase
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uridine diphosphoglucose-protein glucosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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
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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
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?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
UDP-xylose + glycogenin
UDP + xylosylated glycogenin
show the reaction diagram
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autoglycosylation reaction
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?
additional information
?
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the enzyme performs autoglucosylation
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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
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?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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Km-values for UDP-glucose in different tissues
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
unlike mice, humans and other primates have a second variant of glycogenin called glycogenin-2, which is mainly expressed in the liver
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLYG_MOUSE
333
0
37402
Swiss-Prot
other Location (Reliability: 4)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alkali-stable
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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development of assay method with n-dodecyl-beta-D-maltoside as substrate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meezan, E.; Manzella, S.; Roden, L.
Menage a trois: glycogenin, proteoglycan core protein xylosyltransferase and UDP-xylose
Trends Glycosci. Glycotechnol.
7
303-332
1995
Bos taurus, Coturnix sp., Gallus gallus, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
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Manually annotated by BRENDA team
Oldfors, A.
Is glycogenin essential for glycogen synthesis?
Cell Metab.
26
12-14
2017
Homo sapiens (O15488), Homo sapiens (P46976), Mus musculus (Q9R062)
Manually annotated by BRENDA team