Cloned (Comment) | Organism |
---|---|
- |
Klebsiella pneumoniae |
Crystallization (Comment) | Organism |
---|---|
sitting drop method, crystal structures of both the choline-bound and choline free forms of CutC are determined, binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure. Choline-bound CutC crystals exhibit an orthorhombic lattice and space group P212121 with 8 molecules in the asymmetric unit. CutC crystals without choline exhibited a monoclinic lattice and space group P21 with 4 molecules in the asymmetric unit | Klebsiella pneumoniae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
124000 | - |
mass spectrometry analysis. The 124-kDa full-length CutC protein is very unstable, with the N-terminal part starting to degrade almost immediately after purification by nickel affinity chromatography | Klebsiella pneumoniae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | A0A0M3KL45 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Klebsiella pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
choline | - |
Klebsiella pneumoniae | trimethylamine + acetaldehyde | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Klebsiella pneumoniae |
Synonyms | Comment | Organism |
---|---|---|
cutC | - |
Klebsiella pneumoniae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
21 | - |
assay at | Klebsiella pneumoniae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Klebsiella pneumoniae |