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.
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 |
- |
? |
|
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 |
? |
- |
? |
|
2.4.1.186 |
UDP-alpha-D-glucose + glycogenin |
autoglucosylation by glycogenin-1 |
Homo sapiens |
UDP + alpha-D-glucosylglycogenin |
- |
? |
|
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 |
- |
Homo sapiens |
2.4.1.186 |
hGYG1 |
- |
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 |