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Literature summary for 4.2.2.2 extracted from
- Structural modelling, substrate binding and stability studies of endopectate lyase (PL1B) of family 1 polysaccharide lyase from Clostridium thermocellum (2015), Protein Pept. Lett., 22, 557-568 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| molecular modeling of structure. The substrate binding cleft is formed by the amino acid residues from loops and beta-sheet. The structure is quite stable and compact. Residues Asp151, Arg209, Asn234, Arg236, Tyr271 and Ser272 are the key residues involved during catalysis. Among them Arg209 is responsible for proton abstraction during beta-elimination | Acetivibrio thermocellus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | presence of Ca2+ increases thermostability | Acetivibrio thermocellus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acetivibrio thermocellus | A3DHF2 | - |
- |
| Acetivibrio thermocellus DSM 1237 | A3DHF2 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Cthe_2179 | locus name | Acetivibrio thermocellus |
| PL1B | - |
Acetivibrio thermocellus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 74 | - |
melting temperature | Acetivibrio thermocellus |
| 86 | - |
melting temperature, presence of 0.6 mM Ca2+ | Acetivibrio thermocellus |
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