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Literature summary for 1.14.11.2 extracted from

  • Kivirikko, K.I.; Prockop, D.J.
    Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollagen (1967), Arch. Biochem. Biophys., 118, 611-618.
No PubMed abstract available

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information subcellular distribution, differential centrifugation Gallus gallus
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-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
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
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-
-

Purification (Commentary)

Purification (Comment) Organism
using ammonium sulfate fractionation, fractionation with calcium phosphate gel, fractionation with alumina gel, chromatography on DEAE-Sephadex and polyacrylamide gel filtration Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
embryo
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Gallus gallus
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Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(L-prolylglycyl-L-prolyl)n + 2-oxoglutarate + O2 molecular weight of the peptide substrate: about 4000 Gallus gallus 4-hydroxyproline containing peptide
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?
additional information the enzyme is specific for proline in the second position after glycine, the position in which the hydroxyproline in collagen is found. No reaction with: free proline, glycyl-L-prolyl-L-proline or poly-L-proline II with a molecular weight of about 15000 Gallus gallus ?
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?

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
2-oxoglutarate
-
Gallus gallus
ascorbate
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Gallus gallus