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Literature summary extracted from

  • Chaikuad, A.; Froese, D.; Berridge, G.; Von Delft, F.; Oppermann, U.; Yue, W.
    Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis (2011), Proc. Natl. Acad. Sci. USA, 108, 21028-21033.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.186 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.186 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.186 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 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.186 Mn2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.186 UDP-alpha-D-glucose + glycogenin Homo sapiens autoglucosylation by glycogenin-1 UDP + alpha-D-glucosylglycogenin
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?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.186 Homo sapiens P46976
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.186 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chrmatography Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.186 UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin 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 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.186 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 Homo sapiens ?
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?
2.4.1.186 UDP-alpha-D-glucose + glycogenin autoglucosylation by glycogenin-1 Homo sapiens UDP + alpha-D-glucosylglycogenin
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?

Subunits

EC Number Subunits Comment Organism
2.4.1.186 More 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 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.4.1.186 glycogenin
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Homo sapiens
2.4.1.186 hGYG1
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Homo sapiens

General Information

EC Number General Information Comment Organism
2.4.1.186 malfunction the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive Homo sapiens
2.4.1.186 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 Homo sapiens
2.4.1.186 physiological function glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis Homo sapiens