Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.4.1.4: amylosucrase

This is an abbreviated version!
For detailed information about amylosucrase, go to the full flat file.

Word Map on EC 2.4.1.4

Reaction

sucrose
+
[(1->4)-alpha-D-glucosyl]n
=
D-fructose
+
[(1->4)-alpha-D-glucosyl]n+1

Synonyms

AaAS, ACAS, AmAS, AMS, Amy-1, ASASE, BtAS, CcAS, DGAS, DRAS, DRpAS, glucosyltransferase, sucrose-1,4-alpha-glucan, MaAS, MFAS, More, NPAS, NsAS, sucrose-glucan glucosyltransferase, SyAS

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.4 amylosucrase

Crystallization

Crystallization on EC 2.4.1.4 - amylosucrase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged DgAS, free and in complex with turanose, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 1.97-2.10 A resolution
-
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
-
cocrystallization of E328Q mutant enzyme with maltoheptaose, X-ray structure at 2.2 A resolution
crystal structure of the acid/base catalyst mutant, E328Q, with a covalently bound glucopyranosyl moiety. The structure is refined to a resolution of 2.2 A and shows that binding of the covalent intermediate results in a backbone movement of 1 A around the location of the nucleophile, Asp286
-
crystal structure of wild-type amylosucrase in complex with beta-D-glucose at 1.66 A, crystal structure of E328Q mutant enzyme in complex with sucrose at 2.0 A resolution
-
purified recombinant detagged NpAS in complex with turanose, hanging drop vapor diffusion method, 1:1 v/v ratio of protein, containing 6 mg/ml in 20 mM Tris, pH 8.0, to precipitant solution containing 1.5 M sodium acetate, 0.1 M sodium cacodylate, pH 7.0, 2 weeks, X-ray diffraction structure determination and analysis at 1.85 A resolution
recombinant enzyme, equal amounts of 4 mg/ml enzyme in 150 mM NaCl, 50 mM Tris-HCl, pH 7.0, 1 mM EDTA and 1 mM dithiothreitol and reservoir solution consisting of 30% polyethylene glycol 6000 and 100 mM HEPES, pH 7.0, crystal structure at 1.4 A resolution
the mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A is crystallized by hanging drop vapor diffusion method at 12°C