Literature summary extracted from
Skov, L.K.; Pizzut-Serin, S.; Remaud-Simeon, M.; Ernst, H.A.; Gajhede, M.; Mirza, O.
The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology (2013), Acta Crystallogr. Sect. F, 69, 973-978.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.4.1.4 |
recombinant expression in Escherichia coli strain BL21 |
Deinococcus radiodurans |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.4.1.4 |
purified wild-type and mutant ligand-free enzyme, hanging drop vapour diffusion method, mixing of 0.0025 ml of 3.3 mg/ml protein in 50 mM HEPES, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT, with 0.0025 ml of reservoir solution containing 1 M sodium acetate, 0.1 M imidazole, 0.1 M LiCl, pH 6.5, 4°C, X-ray diffraction structure determination and analysis at 3.15 A resolution, modeling |
Deinococcus radiodurans |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.4.1.4 |
sucrose + [(1->4)-alpha-D-glucosyl]n |
Deinococcus radiodurans |
amylosucrases catalyze the formation of an alpha-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor alpha-1,4-glucan |
D-fructose + [(1->4)-alpha-D-glucosyl]n+1 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.4 |
Deinococcus radiodurans |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.4.1.4 |
recombinant enzyme from Escherichia coli strain BL21 to homogeneity using GST-affinity chromatography followed by dialysis and subsequent tag removal via PreScission protease and reverse affinity chromatography |
Deinococcus radiodurans |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.4.1.4 |
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1 |
the elongation mechanism involves enzyme conformational changes to allow the entry of sucrose to the active site |
Deinococcus radiodurans |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.4 |
sucrose + [(1->4)-alpha-D-glucosyl]n |
amylosucrases catalyze the formation of an alpha-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor alpha-1,4-glucan |
Deinococcus radiodurans |
D-fructose + [(1->4)-alpha-D-glucosyl]n+1 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.4.1.4 |
More |
the putative enzyme interface is primarily mediated by two regions from domain N, residues Thr22, Leu25, Arg26, Arg29 and Tyr30 and residues Glu73, Leu76 and Leu77, which are involved in hydrophobic interactions with the corresponding residues from the second protomer |
Deinococcus radiodurans |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.4.1.4 |
DRAS |
- |
Deinococcus radiodurans |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.4.1.4 |
additional information |
ligand binding causes extensive changes in active-site topology |
Deinococcus radiodurans |