Literature summary for 3.2.1.73 extracted from

Chen, C.C.; Huang, J.W.; Zhao, P.; Ko, T.P.; Huang, C.H.; Chan, H.C.; Huang, Z.; Liu, W.; Cheng, Y.S.; Liu, J.R.; Guo, R.T.
Structural analyses and yeast production of the beta-1,3-1,4-glucanase catalytic module encoded by the licB gene of Clostridium thermocellum (2015), Enzyme Microb. Technol., 71, 1-7.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Pichia pastoris and Escherichia coli, recombinant enzmye expressed in Pichia pastoris shows higher specific activity	Acetivibrio thermocellus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure to 1.95 A resolution. The enzyme folds into a classic GH16 beta-jellyroll architecture which consists of two beta-sheets atop each other, with the substrate-binding cleft lying on the concave side of the inner beta-sheet. Two BisTris propane molecules are in the positive and negative substrate binding sites	Acetivibrio thermocellus

Organism

Organism	UniProt	Comment	Textmining
Acetivibrio thermocellus	A3DBX3	-	-
Acetivibrio thermocellus DSM 1237	A3DBX3	-	-

Synonyms

Synonyms	Comment	Organism
Lic16A	-	Acetivibrio thermocellus
LicB	-	Acetivibrio thermocellus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
80	-	20 min, 80% residual activity	Acetivibrio thermocellus
85	-	5 min, 25% residual activity	Acetivibrio thermocellus

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Release 2023.1 (January 2023)