Literature summary for 3.2.1.196 extracted from

Song, H.; Jung, T.; Park, J.; Park, B.; Myung, P.; Boos, W.; Woo, E.; Park, K.
Structural ratio-rials for the short branched substrato specificity of the glycogen debranching enzyme GlgX (2010), Proteins Struct. Funct. Bioinform., 78, 1847-1855.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.15	-	beta-cyclodextrin-alpha-1,6-linked maltotetraose	pH 7, 37°C	Escherichia coli
1.5	-	beta-cyclodextrin-alpha-1,6-linked maltotriose	pH 7, 37°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P15067	member of glycosyl hydrolase 13 family	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
beta-cyclodextrin-alpha-1,6-linked maltopentaose + H2O	-	Escherichia coli	beta-cyclodextrin + maltopentaose	-	?
beta-cyclodextrin-alpha-1,6-linked maltotetraose + H2O	-	Escherichia coli	beta-cyclodextrin + maltotetraose	-	?
beta-cyclodextrin-alpha-1,6-linked maltotriose + H2O	-	Escherichia coli	beta-cyclodextrin + maltotriose	-	?

Synonyms

Synonyms	Comment	Organism
GlgX	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
38	-	beta-cyclodextrin-alpha-1,6-linked maltotriose	pH 7, 37°C	Escherichia coli
41.7	-	beta-cyclodextrin-alpha-1,6-linked maltotetraose	pH 7, 37°C	Escherichia coli