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

BRENDA support

Literature summary extracted from

  • Tsai, L.C.; Hsiao, C.H.; Liu, W.Y.; Yin, L.M.; Shyur, L.F.
    Structural basis for the inhibition of 1,3-1,4-beta-D-glucanase by noncompetitive calcium ion and competitive Tris inhibitors (2011), Biochem. Biophys. Res. Commun., 407, 593-598.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 expression in Escherichia coli Fibrobacter succinogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.73 mutant W203F of truncated beta-glucanase catalytic domain, residues 1-243, to 1.4 A resolution. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202 Fibrobacter succinogenes

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 W203F mutant of truncated beta-glucanase catalytic domain, residues 1-243. mutant has increased hydrolytic activity. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202 Fibrobacter succinogenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.73 Ca2+ noncompetitive Fibrobacter succinogenes
3.2.1.73 imidazole competitive Fibrobacter succinogenes
3.2.1.73 Tris competitive Fibrobacter succinogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.73 Ca2+ three Ca2+ binding sites are found in the mutant W203F structure. The primary calcium is coordinated to seven atoms in a pentagonal-bipyramidal arrangement: three backbone carbonyl oxygen atoms (Asn164, Asn189 and Gly222), one Odelta2 atom of Asn164 and three water molecules. The primary calcium binding site present in the mutant W203F structure is similar to that for the wild-type Fibrobacter succinogenes

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Fibrobacter succinogenes P17989
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 lichenan + H2O
-
 Fibrobacter succinogenes ?
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.73 20.7
-
 Ca2+ mutant W203F, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes
3.2.1.73 23.9
-
 Ca2+ wild-type, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes
3.2.1.73 98.7
-
 imidazole wild-type, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes
3.2.1.73 100.7
-
 Tris mutant W203F, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes
3.2.1.73 117
-
 imidazole mutant W203F, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes
3.2.1.73 255.4
-
 Tris wild-type, pH 6.0, temperature not specified in the publication Fibrobacter succinogenes