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Literature summary extracted from

  • Tuderman, L.; Oikarinen, A.; Kivirikko, K.I.
    Tetramers and monomers of prolyl hydroxylase in isolated chick-embryo tendon cells. The association of inactive monomers to active tetramers and a preliminary characterization of the intracellular monomer-size protein (1977), Eur. J. Biochem., 78, 547-556.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.11.2 bovine serum albumin activation Gallus gallus
1.14.11.2 catalase activation Gallus gallus
1.14.11.2 dithiothreitol activation Gallus gallus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 dithiothreitol 95-100% inhibition at 0.45 mM Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.2 Fe2+
-
 Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.2 Gallus gallus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.2 embryo
-
 Gallus gallus
-
1.14.11.2 tendon embryo Gallus gallus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.11.2 additional information
-
 specific activity of the enzyme in the presence and absence of dithiothreitol Gallus gallus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.2 (Pro-Pro-Gly)n + 2-oxoglutarate + O2 n: 1,5,10 Gallus gallus (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 n: 1,5,10 ?
1.14.11.2 additional information thermal denaturing of the triple-helical conformation of the substrate before hydroxylation Gallus gallus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.2 More about 65% of the enzyme is present in the form of active enzyme tetramers, and about 35% in a form corresponding in molecular weight to the enzyme monomers when studied by gel filtration. The monomer-size protein in the cell represents, at least in part, precursors of the enzyme tetramers, and it can be associated to active tetramers after its ribosomal biosynthesis Gallus gallus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.11.2 37
-
 assay at Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate
-
 Gallus gallus