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Literature summary for 1.14.11.4 extracted from

  • Kivirikko, K.I.; Myllylä, R.
    The hydroxylation of prolyl and lysyl residues (1980), Enzymol. Post- transl. Modif. Proteins (Freedman, R. B. , Hawkins, H. C. , eds. ) Academic Press, New York, 1, 53-104.
No PubMed abstract available

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
-
Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
collagen + 2-oxoglutarate + O2 Gallus gallus
-
5-hydroxylysyl-collagen + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
[procollagen]-L-lysine + 2-oxoglutarate + O2 = [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 mechanism Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
collagen + 2-oxoglutarate + O2
-
Gallus gallus 5-hydroxylysyl-collagen + succinate + CO2
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2 minimum sequence required: Xaa-Lys-Gly Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2 in e.g. lysinevasopressin, lysine-rich histone Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
?

Subunits

Subunits Comment Organism
dimer
-
Gallus gallus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
Gallus gallus