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Literature summary for 1.14.11.2 extracted from

  • Vasta, J.D.; Raines, R.T.
    Collagen prolyl 4-hydroxylase as a therapeutic target (2018), J. Med. Chem., 61, 10403-10411 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.2

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Gallus gallus
Fe2+ required 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 Gallus gallus
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2
-
 Gallus gallus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
procollagen L-proline + 2-oxoglutarate + O2
-
 Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
collagen prolyl 4-hydroxylase
-
 Gallus gallus
collagen prolyl 4-hydroxylase
-
 Homo sapiens
CP4H
-
 Gallus gallus
CP4H
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function (2S,4R)-4-hydroxyproline residues are essential for the stability of this triple helix. These residues arise from the post-translational modification of (2S)-proline residues by collagen prolyl 4-hydroxylases (CP4Hs) Gallus gallus
physiological function (2S,4R)-4-hydroxyproline residues are essential for the stability of this triple helix. These residues arise from the post-translational modification of (2S)-proline residues by collagen prolyl 4-hydroxylases (CP4Hs) Homo sapiens