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Literature summary for 4.1.1.39 extracted from
- Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase (2005), Biochemistry, 44, 113-120.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| determination of crystal structures of L290F and L290F/A222T mutant enzymes to 2.3 A and 2.05 A resolution, hanging-drop vapor diffusion method at 20°C, crystals belong to space group P2(1). Cell dimensions of L290F: a = 121.0 A, b = 177.7 A, c = 122.7 A, beta = 117.7°. Cell dimensions of L290F/A222T: a = 126.0 A, b = 178.2 A, c = 120.5 A, beta = 120.5 A | Chlamydomonas reinhardtii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L290F | mutation causes 13% decrease in CO2/O2 specificity and reduced thermal stability | Chlamydomonas reinhardtii |
| L290F/A222T | A222T mutation suppresses the deleterious effects of the L290F mutation to produce a revertant enzyme with improved thermal stability and kinetic properties virtually indistinguishable from that of the wild-type enzyme | Chlamydomonas reinhardtii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlamydomonas reinhardtii | - |
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