Crystallization (Comment) | Organism |
---|---|
comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability | Proteus mirabilis |
diffraction to 1.96 A. Comparison with catalase from Proteus mirabilis. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. The reduced thermal stability of cold-adapted Aliivibrio salmonicida catalase may be explained by a reduced number of ion-pair networks and displacement of the four C-terminal alpha-helices | Aliivibrio salmonicida LFI1238 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aliivibrio salmonicida LFI1238 | Q3LSM1 | - |
- |
Proteus mirabilis | P42321 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Aliivibrio salmonicida LFI1238 | |
heme | - |
Proteus mirabilis |