3.2.1.196: limit dextrin alpha-1,6-maltotetraose-hydrolase
This is an abbreviated version!
For detailed information about limit dextrin alpha-1,6-maltotetraose-hydrolase, go to the full flat file.
Reaction
Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin. =
Synonyms
GDE, GlgX, GlgX protein, glycogen debranching enzyme, isoamylase-type debranching enzyme
ECTree
3.2.1.196 limit dextrin alpha-1,6-maltotetraose-hydrolaseAdvanced search results
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results (Crystallization
Crystallization on EC 3.2.1.196 - limit dextrin alpha-1,6-maltotetraose-hydrolase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M sodium citrate, 47% (v/v) MPD, 4% (v/v) PEG 3350, and HEPES (pH 8.0) buffer
hanging drop vapor diffusion method, using 0.2 M sodium citrate, 47% (w/v) 2-methyl-2,4-pentanediol, 4% (w/v) PEG 3350, and HEPES (pH 8.0) buffer
to 2.25 A resolution. Structure reveals a monomer consisting of three major domains with high structural similarity to the subunit of TreX, the oligomeric bifunctional glycogen debranching enzyme from Sulfolobus. In the overlapping substrate binding groove, conserved residues Leu270, Asp271, and Pro208 block the cleft, yielding a shorter narrow GlgX cleft compared to that of TreX. Residues 207-213 form a unique helical conformation that is observed in both GlgX and TreX, possibly distinguishing GDEs from isoamylases and pullulanases
