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Literature summary for 1.14.11.2 extracted from

  • Gorres, K.L.; Pua, K.H.; Raines, R.T.
    Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase (2009), PLoS ONE, 4, e7635.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain Origami DE3 Homo sapiens

Protein Variants

Protein Variants Comment Organism
D414A site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive Homo sapiens
D414G site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive Homo sapiens
D414H site-directed mutagenesis, the mutation mimics the active site of a cysteine dioxygenase, the mutant is inactive Homo sapiens
D414H/H483D site-directed mutagenesis, the mutant is inactive Homo sapiens
H412D/D414H site-directed mutagenesis, the mutant is inactive Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
potassium bromide over 80% inhibition at 500 mM Homo sapiens
potassium chloride over 80% inhibition at 500 mM Homo sapiens
potassium fluoride over 90% inhibition at 500 mM Homo sapiens
potassium iodide over 80% inhibition at 500 mM Homo sapiens
sodium bromide over 80% inhibition at 500 mM Homo sapiens
sodium chloride over 80% inhibition at 500 mM Homo sapiens
sodium iodide over 90% inhibition at 500 mM Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required cofactor, residues His412, Asp414, and His483 form an iron-coordinating 2-His-1-carboxylate motif, high stringency for the iron-binding residues in the P4H active site, mechanism, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Origami DE3 Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism with Fe2+ bound in the active site by a 2-His-1-Asp motif, overview Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2 P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
procollagen L-proline + 2-oxoglutarate + O2 high stringency for the iron-binding residues in the P4H active site, structure-function relationship, overview Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Subunits

Subunits Comment Organism
tetramer alpha2beta2, catalytic alpha subunit Homo sapiens

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the alpha-ketoglutarate-dependent iron(II) dioxygenases Homo sapiens
P4H
-
 Homo sapiens
prolyl 4-hydroxylase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Homo sapiens