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.
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 4.54.7, and 1013% (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 |