Crystallization (Comment) | Organism |
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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 | Organism |
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stable protein even at high concentrations of chaotropic agents | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | Q5JDJ7 | member of family GH57 | - |
Renatured (Comment) | Organism |
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unfolding equilibrium is a two-state process with no intermediates | Thermococcus kodakarensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
TK1436 | - |
Thermococcus kodakarensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
high thermal tolerance even at boiling temperatures | Thermococcus kodakarensis |