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Literature summary for 1.14.11.2 extracted from

  • Culpepper, M.; Scott, E.; Limburg, J.
    Crystal structure of prolyl 4-hydroxylase from Bacillus anthracis (2010), Biochemistry, 49, 124-133.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified SeMet anthrax P4H, hanging drop vapor diffusion method, 24 mg/mL protein in 50 mM Tris, pH 7.4, containing 150 mM KCl and 5 mM 2-mercaptoethanol, is mixed with and equal volume of well solution containing 16% w/v PEG 8000, 40 mM potassium phosphate, pH 4.0-4.2, and 20% v/v glycerol, at 20°C, under aerobic conditions, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.4 A resolution Bacillus anthracis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for activity, binds in a conserved facial triad binding site, His1-X-Asp/Glu-Xn-His2 Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2 Bacillus anthracis
-
?
-
?
procollagen L-proline + 2-oxoglutarate + O2 Bacillus anthracis
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81LZ8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
-
Bacillus anthracis ?
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Bacillus anthracis procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 substrate binding and active site structure, overview Bacillus anthracis procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Subunits

Subunits Comment Organism
More the enzyme possesses the double-stranded beta-helix core fold characteristic of Fe(II)/2-oxoglutarate oxygenases, that positions Fe-binding and 2-oxoglutarate-binding residues in what is expected to be catalytically competent orientations and is consistent with proline peptide substrate binding at the active site mouth Bacillus anthracis

Synonyms

Synonyms Comment Organism
P4H
-
Bacillus anthracis
prolyl 4-hydroxylase
-
Bacillus anthracis

General Information

General Information Comment Organism
physiological function prolyl 4-hydroxylase catalyzes the post-translational hydroxylation of proline residues and plays a role in collagen production, hypoxia response, and cell wall development Bacillus anthracis