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Literature summary for 1.14.11.2 extracted from

  • De Waal, A.; de Jong, L.
    Processive action of the two peptide binding sites of prolyl 4-hydroxylase in the hydroxylation of procollagen (1988), Biochemistry, 27, 150-155.
    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
catalase activation Gallus gallus
dithiothreitol activation Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5 loss of enzyme activity with (Pro-Pro-Gly)5 as a substrate upon photoaffinity labeling Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information effect of photoaffinity labeling with N-(4-azido-2-nitrophenyl)glycyl-(Pro-Pro-Gly)5, substrates: (Pro-Pro-Gly)5 or procollagen Gallus gallus

Organism

Organism UniProt Comment Textmining
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 ?
procollagen L-proline + 2-oxoglutarate + O2
-
 Gallus gallus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Gallus gallus