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Literature summary for 1.14.11.2 extracted from

  • De Jong, L.; van der Kraan, I.; de Waal, A.
    The kinetics of the hydroxylation of procollagen by prolyl 4-hydroxylase. Proposal for a processive mechanism of binding of the dimeric hydroxylating enzyme in relation to the high kcat/Km ratio and a conformational requirement for hydroxylation of -X-Pro-Gly- sequences (1991), Biochim. Biophys. Acta, 1079, 103-111.
    View publication on PubMed
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Activating Compound

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000016
-
 Procollagen L-proline
-
 Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 mechanism Gallus gallus
a

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
32
-
 assay at Gallus gallus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.8
-
 Procollagen L-proline
-
 Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
 Gallus gallus
7.7
-
 assay at Gallus gallus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Gallus gallus