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Literature summary for 1.14.11.4 extracted from

  • Turpeenniemi-Hujanen, T.M.; Puistola, U.; Kivirikko, K.I.
    Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein (1980), Biochem. J., 189, 247-253.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
loss of activity during concentration Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Gallus gallus 5783
-

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
two alternative procedures Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Gallus gallus

Storage Stability

Storage Stability Organism
-20°C, enzyme purified by collagen-agarose column-chromatography stable, enzyme from Bio-gel column unstable Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidyl-L-lysine + 2-oxoglutarate + O2 protocollagen Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2 hydroxy-L-lysine ?
[procollagen]-L-lysine + 2-oxoglutarate + O2
-
Gallus gallus [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
r

Subunits

Subunits Comment Organism
dimer 2 * 83000-85000, SDS-PAGE Gallus gallus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6 4.2 [procollagen]-L-lysine in synthetic peptides Gallus gallus