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Literature summary for 1.14.11.4 extracted from

  • Puistola, U.; Turpeenniemi-Hujanen, T.M.; Myllylä, R.; Kivirikko, K.I.
    Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects (1980), Biochim. Biophys. Acta, 611, 40-50.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine can replace ascorbate Gallus gallus
2-mercaptoethanol can replace ascorbate Gallus gallus
dithiothreitol can replace ascorbate Gallus gallus
L-cysteine can replace ascorbate Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04 0.05 O2
-
Gallus gallus
0.05
-
2-oxoglutarate
-
Gallus gallus
0.09 0.12 2-oxoglutarate
-
Gallus gallus
0.19 0.22 ascorbate
-
Gallus gallus
0.4 0.5 Procollagen L-lysine
-
Gallus gallus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
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.
2-oxoglutarate + O2 + ascorbate uncoupled decarboxylation in absence of peptide substrate Gallus gallus succinate + CO2 + dehydroascorbate + H2O
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
-
Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
?
[procollagen] L-lysine + 2-oxoglutarate + O2
-
Gallus gallus [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
r

Cofactor

Cofactor Comment Organism Structure
ascorbate required Gallus gallus