Literature summary for 2.4.1.186 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.

Search for more literature for 2.4.1.186

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Metals/Ions	Comment	Organism	Structure
Mn2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P46976	-	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
glycogenin	-	Homo sapiens
hGYG1	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive	Homo sapiens
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
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

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Release 2023.1 (January 2023)