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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.196 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.196 0.15
-
beta-cyclodextrin-alpha-1,6-linked maltotetraose pH 7, 37°C Escherichia coli
3.2.1.196 1.5
-
beta-cyclodextrin-alpha-1,6-linked maltotriose pH 7, 37°C Escherichia coli

Organism

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.2.1.196 GlgX
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.196 38
-
beta-cyclodextrin-alpha-1,6-linked maltotriose pH 7, 37°C Escherichia coli
3.2.1.196 41.7
-
beta-cyclodextrin-alpha-1,6-linked maltotetraose pH 7, 37°C Escherichia coli