Literature summary extracted from
Santos, C.; Tonoli, C.; Trindade, D.; Betzel, C.; Takata, H.; Kuriki, T.; Kanai, T.; Imanaka, T.; Arni, R.; Murakami, M.
Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (2011), Proteins, 79, 547-557.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.4.1.18 |
in the native state and in complex with glucose and substrate mimetics, to 2.4 A, 2.9 A, and 1.9 A resolution, respectively. The structure encompasses a distorted (beta/alpha)7-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233, which is fully conserved among GH13- and GH57-type branching enzymes |
Thermococcus kodakarensis |
General Stability
EC Number |
General Stability |
Organism |
---|
2.4.1.18 |
stable protein even at high concentrations of chaotropic agents |
Thermococcus kodakarensis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.18 |
Thermococcus kodakarensis |
Q5JDJ7 |
member of family GH57 |
- |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
2.4.1.18 |
unfolding equilibrium is a two-state process with no intermediates |
Thermococcus kodakarensis |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.18 |
additional information |
loop 220-245, named as catalytic loop, acts as a lid retaining the intermediate reaction product for subsequent transfer to a new a-1,6 position. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233 |
Thermococcus kodakarensis |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.4.1.18 |
TK1436 |
- |
Thermococcus kodakarensis |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
2.4.1.18 |
additional information |
- |
high thermal tolerance even at boiling temperatures |
Thermococcus kodakarensis |