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Literature summary extracted from

  • Hurley, T.D.; Stout, S.; Miner, E.; Zhou, J.; Roach, P.J.
    Requirements for catalysis in mammalian glycogenin (2005), J. Biol. Chem., 280, 23892-23899.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.186 expression of wild-type and mutant enzymes in Saccharomyces cerevisiae Oryctolagus cuniculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.186 the DELTA270 enzyme crystallizes at 7.5 mg/ml from solutions containing 1 mM UDP-glucose, 1 mM MnCl2, 100 mM sodium acetate, pH 4.5–4.7, and 10–13% (w/v) PEG 4000 in the space group P64, with cell dimensions a = b = 75.0, c = 233.4, gamma = 120° and a dimer in the asymmetric unit. All crystals are grown using hanging drop vapor diffusion methods at 23°C Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.186 D159N exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer, self-glucosylation activities below the limit of detection of the assay. Ability to catalyze the transglucosylation of maltose is reduced by 260fold, hydrolysis of UDP-glucose is reduced 12fold Oryctolagus cuniculus
2.4.1.186 D159S stable enzyme, self-glucosylation activities below the limit of detection of the assay. Transglucosylation activity of the mutant enzyme is reduced to undetectable levels, activity for the hydrolysis of UDP-glucose is reduced 14fold Oryctolagus cuniculus
2.4.1.186 D162N exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer, self-glucosylation activities below the limit of detection of the assay, undetectable activity for the transglucosylation of maltose and the hydrolysis of UDP-glucose to free glucose Oryctolagus cuniculus
2.4.1.186 D162S stable enzyme, self-glucosylation activities below the limit of detection of the assay. 30fold less active for the trans-glucosylation of maltose and 340fold less active for the hydrolysis of UDP-glucose Oryctolagus cuniculus
2.4.1.186 DELTA270-332 mutant enzyme is fully active, specific activity for self- or transglucosylation is indistinguishable from the full-length enzyme Oryctolagus cuniculus
2.4.1.186 DELTA270-332/D159S inactive mutant enzyme Oryctolagus cuniculus
2.4.1.186 DELTA270-332/D162N exists as both tetrameric and dimeric species, compared to wild-type enzyme which exists to more than 95% as dimer Oryctolagus cuniculus
2.4.1.186 DELTA270-332/D162S 18fold less active for the transglucosylation of maltose and 190fold less active for the hydrolysis of UDP-glucose than wild-type enzyme, activity for the hydrolysis of UDP-glucose is reduced 4fold Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.186 58000
-
truncation mutant enzymes DELTA270-332/D159S and DELTA270-332/D162S, gel filtration Oryctolagus cuniculus
2.4.1.186 103000
-
wild-type enzyme in glycosylated and nonglycosylated form, full-length mutant enzymes D162S and D159S, gel filtration Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.186 Oryctolagus cuniculus P13280
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.186 glycoprotein
-
Oryctolagus cuniculus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.186 wild-type and mutant enzymes Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.186 muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.186 UDP-glucose + glycogenin self-glucosylation Oryctolagus cuniculus UDP + glucosylglycogenin
-
?
2.4.1.186 UDP-glucose + maltose trans-glucosylation. 93% of the transferred glucose molecules appears in maltotriose, 6% are attached to glycogenin, and 1% is liberated as free glucose Oryctolagus cuniculus UDP + maltotriose
-
?

Subunits

EC Number Subunits Comment Organism
2.4.1.186 dimer truncation mutant enzymes DELTA270-332/D159S and DELTA270/D162S, wild-type enzyme in glycosylated and nonglycosylated form, full-length mutant enzymes D162S and D159S exists as more than 95% dimer. Mutant enzymes D159N, D162N and DELTA270-332/D162N exist as both tetrameric and dimeric species Oryctolagus cuniculus
2.4.1.186 tetramer mutant enzymes D159N, D162N and DELTA270-332/D162N exist as both tetrameric and dimeric species Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
2.4.1.186 glycogenin
-
Oryctolagus cuniculus