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

BRENDA support

Literature summary extracted from

  • Puistola, U.
    Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types (1982), Biochem. J., 201, 215-219.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.4 additional information
-
 additional information comparison of Km of 2-oxoglutarate, ascorbate, Fe2+ and type I, type II and type IV protocollagen as substrate with type I, type II and type IV enzyme Gallus gallus
1.14.11.4 additional information
-
 additional information comparison of Km of 2-oxoglutarate, ascorbate, Fe2+ and type I, type II and type IV protocollagen as substrate with type I, type II and type IV enzyme Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.4 Fe2+ required, Km: 0.001-0.005 mM Gallus gallus
1.14.11.4 Fe2+ required, Km: 0.001-0.005 mM Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.4 Gallus gallus
-
-
-
1.14.11.4 Homo sapiens
-
 HT 1080 sarcoma cells
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.4 embryo
-
 Homo sapiens
-
1.14.11.4 embryo tendons and sterna Gallus gallus
-
1.14.11.4 additional information collagen type-specific isoenzymes Gallus gallus
-
1.14.11.4 additional information collagen type-specific isoenzymes Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.4 peptidyl-L-lysine + 2-oxoglutarate + O2
-
 Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
 ?
1.14.11.4 peptidyl-L-lysine + 2-oxoglutarate + O2
-
 Homo sapiens peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.4 ascorbate required Gallus gallus
1.14.11.4 ascorbate required Homo sapiens