Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.11.2 extracted from

  • Miller, M.A.; Scott, E.E.; Limburg, J.
    Expression, purification, crystallization and preliminary X-ray studies of a prolyl-4-hydroxylase protein from Bacillus anthracis (2008), Acta Crystallogr. Sect. F, 64, 788-791.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of selenomethionine-labeled anthrax-P4H in Escherichia coli strain BL21(DE3) Bacillus anthracis

Crystallization (Commentary)

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michalis-Menten kinetics Bacillus anthracis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Bacillus anthracis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
gel filtration, recombinant enzyme Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant selenomethionine-labeled anthrax-P4H from Escherichia coli by anion exchange chromatography and gel filtration toover 99% purity Bacillus anthracis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
-
Bacillus anthracis ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 x 27000, recombinant enzyme, SDS-PAGE Bacillus anthracis

Synonyms

Synonyms Comment Organism
anthrax-P4H
-
Bacillus anthracis
C-P4H
-
Bacillus anthracis
collagen prolyl-4-hydroxylase
-
Bacillus anthracis

General Information

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