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Literature summary extracted from

  • De Jong, L.; Albracht, S.P.J.; Kemp., A.
    Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation (1982), Biochim. Biophys. Acta, 704, 326-332.
    View publication on PubMed

Activating Compound

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 3,4-dihydroxybenzoate
-
 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
-

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
-
 effect of preincubation with 2-oxoglutarate on the rate and extent of oxygen uptake by the ascorbate-independent enzyme activity Gallus gallus
1.14.11.2 2.4
-
 ascorbate added before the addition of 2-oxoglutarate 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 ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.2 7.7
-
 assay at Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate
-
 Gallus gallus
1.14.11.2 additional information analysis of the activity in the absence and presence of ascorbate Gallus gallus