Literature summary for 3.2.1.73 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.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Fibrobacter succinogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
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

Inhibitors	Comment	Organism
Ca2+	noncompetitive	Fibrobacter succinogenes
imidazole	competitive	Fibrobacter succinogenes
Tris	competitive	Fibrobacter succinogenes

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Fibrobacter succinogenes	P17989	-	-

Substrates and Products (Substrate)

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

Ki Value [mM]

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