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Literature summary for 1.14.11.4 extracted from

  • Miller, R.L.; Varner, H.H.
    Purification and enzymatic properties of lysyl hydroxylase from fetal procine skin (1979), Biochemistry, 18, 5928-5932.
No PubMed abstract available
Search for more literature for 1.14.11.4

Activating Compound

Activating Compound Comment Organism Structure
bovine serum albumin activation Sus scrofa
catalase activation Sus scrofa
dithiothreitol
-
 Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide
-
 Sus scrofa
N-ethylmaleimide
-
 Sus scrofa
p-chloromercuribenzoate
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 x * 70000 + x * 115000, SDS-PAGE Sus scrofa
115000
-
 x * 70000 + x * 115000, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
skin fetus Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidyl-L-lysine + 2-oxoglutarate + O2 protocollagen Sus scrofa peptidyl-5-hydroxy-L-lysine + succinate + CO2 hydroxy-L-lysine ?

Subunits

Subunits Comment Organism
? x * 70000 + x * 115000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Sus scrofa