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Literature summary for 1.14.11.7 extracted from

  • Risteli, J.; Tryggvason, K.; Kivirikko, K.I.
    A rapid assay for prolyl 3-hydroxylase activity (1978), Anal. Biochem., 84, 423-431.
    View publication on PubMed
Search for more literature for 1.14.11.7

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000034
-
 Procollagen
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen + 2-oxoglutarate + O2 Rattus norvegicus the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 rapid assay method Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen + 2-oxoglutarate + O2 the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues Rattus norvegicus procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
 ?
procollagen L-proline + 2-oxoglutarate + O2 2,3-T-L-proline-labeled polypeptide substrate Rattus norvegicus procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
 ?

Cofactor

Cofactor Comment Organism Structure
ascorbate required Rattus norvegicus