Literature summary for 3.2.1.4 extracted from

Jeng, W.Y.; Liu, C.I.; Lu, T.J.; Lin, H.J.; Wang, N.C.; Wang, A.H.
Crystal structures of the C-terminally truncated endoglucanase Cel9Q from Clostridium thermocellum complexed with cellodextrins and Tris (2019), ChemBioChem, 20, 295-307 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene celQ, sequence comparisons, recombinant expression of truncated and point mutant enzymes in Escherichia coli strain BL21(DE3)	Acetivibrio thermocellus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant C-terminally truncated mutant enzyme CtCel9QDELTAc complexed with Tris, Tris + cellobiose, cellobiose + cellotriose, cellotriose, and cellotetraose, sitting drop vapor diffusion method, a drop consists of 0.0013 ml of protein solution and 0.0013 ml of reservoir solution containing 9-12% w/v PEG 3350, 15-20% v/v PEG 550MME, 30 mM NaBr, 30 mM NaF, and 30 mM NaI, and 0.1 M Tris, pH 8.5, with or without 10 mM cellooligosaccharides, equilibration against 0.2 ml reservoir solution, 22°C, X-ray diffraction structure determination analysis at resolutions 1.50, 1.70, 2.05, 2.05, and 1.75 A, respectively. In both the oligosaccharide-free and cellobiose-bound CtCel9QDELTAc structures, a Tris molecule is observed in the active site	Acetivibrio thermocellus

Crystallization (Comment)

Organism

purified recombinant C-terminally truncated mutant enzyme CtCel9QDELTAc complexed with Tris, Tris + cellobiose, cellobiose + cellotriose, cellotriose, and cellotetraose, sitting drop vapor diffusion method, a drop consists of 0.0013 ml of protein solution and 0.0013 ml of reservoir solution containing 9-12% w/v PEG 3350, 15-20% v/v PEG 550MME, 30 mM NaBr, 30 mM NaF, and 30 mM NaI, and 0.1 M Tris, pH 8.5, with or without 10 mM cellooligosaccharides, equilibration against 0.2 ml reservoir solution, 22°C, X-ray diffraction structure determination analysis at resolutions 1.50, 1.70, 2.05, 2.05, and 1.75 A, respectively. In both the oligosaccharide-free and cellobiose-bound CtCel9QDELTAc structures, a Tris molecule is observed in the active site

Acetivibrio thermocellus

Protein Variants

Protein Variants	Comment	Organism
D79A	site-directed mutagenesis	Acetivibrio thermocellus
E435A	site-directed mutagenesis	Acetivibrio thermocellus
additional information	construction of a C-terminally truncated enzyme, CtCel9QDELTAc	Acetivibrio thermocellus

Inhibitors

Inhibitors	Comment	Organism	Structure
Tris	Tris almost completely suppresses CtCel9Q hydrolase activity, a Tris molecule is bound to three catalytic residues of CtCel9Q and occupies subsite -1 of the CtCel9Q active-site cleft, enzyme mutant crystal structure analysis, overview	Acetivibrio thermocellus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	two endogenous calcium ions are observed in the calcium-binding sites of all CtCel9QDELTAc structures, enzyme mutant structure analysis, overview	Acetivibrio thermocellus

Organism

Organism	UniProt	Comment	Textmining
Acetivibrio thermocellus	Q9AJF8	i.e. Ruminiclostridium thermocellum	-

Subunits

Subunits	Comment	Organism
More	the precursor form of CtCel9Q comprises a signal peptide, a glycoside hydrolase family 9 catalytic domain, a type 3c carbohydrate-binding module (CBM), and a type I dockerin domain	Acetivibrio thermocellus

Synonyms

Synonyms	Comment	Organism
Cel9Q	-	Acetivibrio thermocellus
endoglucanase	-	Acetivibrio thermocellus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	-	Acetivibrio thermocellus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
35	75	over 50% of maximal activity within this range, profile overview	Acetivibrio thermocellus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	-	Acetivibrio thermocellus

pH Range

pH Minimum	pH Maximum	Comment	Organism
4	7.5	over 50% of maximal activity within this range, profile overview	Acetivibrio thermocellus