Cloned (Comment) | Organism |
---|---|
gene GBAA_4459, recombinant enzyme expression in Escherichia coli strain BL21 Star (DE3) pLysS | Bacillus anthracis |
Crystallization (Comment) | Organism |
---|---|
purified enzyme BaP4H complexed with cadmium or 2-oxoglutarate, mixing of 0.001 ml of 9 mg/ml protein solution containing 1 mM CoCl2 and 1 mM 2-oxoglutarate with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.8, 0.05 M cadmium sulfate, and 0.9 M sodium acetate, equilibration against 0.35 ml of reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.63 and 2.35 A resolution, respectively, soaking of the different crystals in different cryoprotection solutions, molecular replacement using the monomer (chain A), PDB Id 3itq, as a starting model | Bacillus anthracis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cd2+ | the binding of Cd2+ induces a conformational change in the enzyme structure compared to the wild-type enzyme, overview | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a non-heme iron enzyme, required for catalysis | Bacillus anthracis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | Bacillus anthracis | - |
procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | Q81LZ8 | alpha-subunit domain protein | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from by a process involving hydrophobic interaction chromatography purification step prior to gel filtration | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | - |
Bacillus anthracis | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BaP4H | - |
Bacillus anthracis |
GBAA_4459 | - |
Bacillus anthracis |
P4H | - |
Bacillus anthracis |
prolyl 4-hydroxylase | - |
Bacillus anthracis |
General Information | Comment | Organism |
---|---|---|
metabolism | the stabilization of collagen triple-helical structure via prolyl hydroxylation involving the enzyme is the rate-limiting step in collagen biosynthesis | Bacillus anthracis |
additional information | active site structure and substrate recognition, overview | Bacillus anthracis |
physiological function | prolyl 4-hydroxylases are mononuclear nonheme iron enzymes that catalyze the formation of 4R-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation. The stabilization of collagen triple-helical structure via prolyl hydroxylation is the rate-limiting step in collagen biosynthesis | Bacillus anthracis |