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Literature summary for 1.14.11.2 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
Search for more literature for 1.14.11.2

Activating Compound

Activating Compound Comment Organism Structure
bovine serum albumin activation Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
3,4-dihydroxybenzoate
-
 Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Gallus gallus

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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 ?
additional information thermal denaturing of the triple-helical conformation of the substrate before hydroxylation Gallus gallus ?
-
 ?

pH Optimum

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

Cofactor

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