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Literature summary for 2.4.1.186 extracted from

  • Carrizo, M.; Romero, J.; Issoglio, F.; Curtino, J.
    Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation (2012), FEBS Lett., 586, 254-257.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type gycogenin-1, its truncated mutant DELTA-270, and of glycogenin-1 point mutants in Escherichia coli strain CGSC 4997 Oryctolagus cuniculus

Crystallization (Commentary)

Crystallization (Comment) Organism
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, 4°C, crystals are soaked in mother liquor containing 1 mM MnSO4 and 1 mM UDP or UDP-glucose, X-ray diffraction structure determination and analysis Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
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 Oryctolagus cuniculus
T83S site-directed mutagenesis, the mutant is catalytically active Oryctolagus cuniculus
T83V site-directed mutagenesis, inactive mutant Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P13280
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type gycogenin-1, its truncated mutant DELTA-270, and of glycogenin-1 point mutants from Escherichia coli strain CGSC 4997 Oryctolagus cuniculus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glycogenin-1
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Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Oryctolagus cuniculus

General Information

General Information Comment Organism
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 Oryctolagus cuniculus
physiological function Asp162 is the residue involved in the activation step of the glucose transfer reaction mechanism Oryctolagus cuniculus