Literature summary for 3.2.1.4 extracted from

Cheng, Y.; Ko, T.; Wu, T.; Ma, Y.; Huang, C.; Lai, H.; Wang, A.; Liu, J.; Guo, R.
Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima (2011), Proteins, 79, 1193-1204.

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutant E134C free or in complex crystals with cellotetraose and cellobiose, sitting drop vapor diffusion method for the wild-type enzyme usage of a reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 10% glycerol, and 15% PEG 3350, for the mutant E134C a reservoir solution containing 0.1 M ammonium sulfate, 0.1 M Bis-Tris, pH 5.5, 5% glycerol, and 18% PEG 3350 is used, addition of 10 mM cellobiose or cellotetraose, room temperature, 2 days, X-ray diffraction structure determination and analysis at 1.47-2.09 A resolution	Thermotoga maritima

Crystallization (Comment)

Organism

wild-type and mutant E134C free or in complex crystals with cellotetraose and cellobiose, sitting drop vapor diffusion method for the wild-type enzyme usage of a reservoir solution containing 0.1 M Bis-Tris, pH 5.5, 10% glycerol, and 15% PEG 3350, for the mutant E134C a reservoir solution containing 0.1 M ammonium sulfate, 0.1 M Bis-Tris, pH 5.5, 5% glycerol, and 18% PEG 3350 is used, addition of 10 mM cellobiose or cellotetraose, room temperature, 2 days, X-ray diffraction structure determination and analysis at 1.47-2.09 A resolution

Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
E134C	site-directed mutagenesis, the catalytically inactive active-site mutant adopts a beta-jellyroll protein fold typical of the GH12-family enzymes, with two curved beta-sheets A and B and a central active-site cleft, crystal structure determination, overview	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q60032	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	substrate-binding mode of cellulase 12A, overview. A network of interactions exists between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the 22 and 21 subsites than in the 11, 12 and 23 subsites. In the E134C crystals the bound 21 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure	Thermotoga maritima	?	-	?

Synonyms

Synonyms	Comment	Organism
beta-1,4-endoglucanase	-	Thermotoga maritima
Cel12A	-	Thermotoga maritima
cellulase 12A	-	Thermotoga maritima
More	the enzyme belongs to the GH12 family of glycoside hydrolases	Thermotoga maritima

General Information

General Information	Comment	Organism
physiological function	cellulase 12A degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate	Thermotoga maritima