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Literature summary for 3.2.1.4 extracted from

  • Gao, J.; Huang, J.W.; Li, Q.; Liu, W.; Ko, T.P.; Zheng, Y.; Xiao, X.; Kuo, C.J.; Chen, C.C.; Guo, R.T.
    Characterization and crystal structure of a thermostable glycoside hydrolase family 45 1,4-beta-endoglucanase from Thielavia terrestris (2017), Enzyme Microb. Technol., 99, 32-37 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Thermothielavioides terrestris

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of apoenzyme and in complex with cellobiose and cellotetraose, to 1.36-1.58 A resolution. The protein folds into two overall regions, one is a six-stranded beta-barrel, and the other one consists of several extended loops. Between the two regions lies the substrate-binding channel, which is an open cleft spanning across the protein surface. A continuous substrate-binding cleft from subsite -4 to +3 canbe identified Thermothielavioides terrestris

Organism

Organism UniProt Comment Textmining
Thermothielavioides terrestris G2QVH7
-
-
Thermothielavioides terrestris ATCC 38088 G2QVH7
-
-

Synonyms

Synonyms Comment Organism
Cel45A
-
Thermothielavioides terrestris
THITE_2110957
-
Thermothielavioides terrestris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Thermothielavioides terrestris

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
80
-
more than 50% of maximum activity Thermothielavioides terrestris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
2.5 h, 80% residual activity Thermothielavioides terrestris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 5
-
Thermothielavioides terrestris