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Literature summary for 1.14.11.4 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
Search for more literature for 1.14.11.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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

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

Organism

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

Source Tissue

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

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
ascorbate required Gallus gallus
ascorbate required Homo sapiens