Cloned (Comment) | Organism |
---|---|
expression of selenomethionine-labeled anthrax-P4H in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
Crystallization (Comment) | Organism |
---|---|
recombinant selenomethionine-labeled anthrax-P4H, hanging-drop vapor-diffusion method, 0.001 ml of 24 mg/ml recombinant protein in 50 mM Tris-HCl, 150 mM KCl, and 5 mM 2-mercaptoethanol, pH 7.4, is mixed with 0.001 ml and equilibrated against 0.75 ml of reservoir solution containing 16% w/v PEG 8000, 40 mM potassium phosphate, and 20% glycerol at 20°C, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michalis-Menten kinetics | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | - |
Bacillus anthracis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
54000 | - |
gel filtration, recombinant enzyme | Bacillus anthracis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant selenomethionine-labeled anthrax-P4H from Escherichia coli by anion exchange chromatography and gel filtration toover 99% purity | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2 | - |
Bacillus anthracis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 x 27000, recombinant enzyme, SDS-PAGE | Bacillus anthracis |
Synonyms | Comment | Organism |
---|---|---|
anthrax-P4H | - |
Bacillus anthracis |
C-P4H | - |
Bacillus anthracis |
collagen prolyl-4-hydroxylase | - |
Bacillus anthracis |
General Information | Comment | Organism |
---|---|---|
physiological function | collagen prolyl-4-hydroxylases, C-P4Hs, are essential enzymes in the post-translational modification of procollagen. C-P4Hs catalyze the hydroxylation of proline residues at the Yaa positions of (Gly-Xaa-Yaa)n repeats in collagen and other proteins containing collagen-like domains, where Xaa is often proline and Yaa is often hydroxyproline | Bacillus anthracis |