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Literature summary extracted from

  • Kivirikko, K.I.; Myllylä, R.; Pihlajaniemi, T.
    Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit (1989), FASEB J., 3, 1609-1617.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 3,4-dihydroxybenzoate
-
 Gallus gallus
1.14.11.2 3,4-dihydroxybenzoate
-
 Homo sapiens
1.14.11.2 Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
 Gallus gallus
1.14.11.2 Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
 Homo sapiens
1.14.11.2 Beta-lactam antibiotics
-
 Gallus gallus
1.14.11.2 Beta-lactam antibiotics
-
 Homo sapiens
1.14.11.2 Coumalic acid i.e. 2-oxo-1,2H-pyran-5-carboxylic acid Gallus gallus
1.14.11.2 Coumalic acid i.e. 2-oxo-1,2H-pyran-5-carboxylic acid Homo sapiens
1.14.11.2 daunorubicin
-
 Gallus gallus
1.14.11.2 daunorubicin
-
 Homo sapiens
1.14.11.2 doxorubicin
-
 Gallus gallus
1.14.11.2 doxorubicin
-
 Homo sapiens
1.14.11.2 ethylpyridine-2,4-dicarboxylate
-
 Gallus gallus
1.14.11.2 ethylpyridine-2,4-dicarboxylate
-
 Homo sapiens
1.14.11.2 N,N'-diethylpyridine 2,4-dicarboxamide
-
 Gallus gallus
1.14.11.2 N,N'-diethylpyridine 2,4-dicarboxamide
-
 Homo sapiens
1.14.11.2 poly(L-proline) competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length Gallus gallus
1.14.11.2 poly(L-proline) competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length Homo sapiens
1.14.11.2 poly(L-proline)
-
 Mus musculus
1.14.11.2 Pyridine 2,4-dicarboxylate
-
 Gallus gallus
1.14.11.2 Pyridine 2,4-dicarboxylate
-
 Homo sapiens
1.14.11.2 Pyridine 2,4-dicarboxylate
-
 Mus musculus
1.14.11.2 Pyridine 2,4-dicarboxylate
-
 Volvox carteri
1.14.11.2 Pyridine 2,5-dicarboxylate
-
 Gallus gallus
1.14.11.2 Pyridine 2,5-dicarboxylate
-
 Homo sapiens
1.14.11.2 Pyridine 2,5-dicarboxylate
-
 Volvox carteri
1.14.11.2 Zn2+
-
 Gallus gallus
1.14.11.2 Zn2+
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.2 0.0002
-
 protocollagen type I L-proline
-
 Gallus gallus
1.14.11.2 0.0002
-
 protocollagen type I L-proline
-
 Homo sapiens
1.14.11.2 0.05
-
 (Pro-Pro-Gly)10
-
 Homo sapiens
1.14.11.2 0.05
-
 (L-Pro-L-Pro-Gly)10
-
 Gallus gallus
1.14.11.2 1.8
-
 (L-Pro-L-Pro-Gly)5
-
 Gallus gallus
1.14.11.2 1.8
-
 (L-Pro-L-Pro-Gly)5
-
 Homo sapiens
1.14.11.2 20
-
 L-Pro-L-Pro-Gly
-
 Gallus gallus
1.14.11.2 20
-
 L-Pro-L-Pro-Gly
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.2 Fe2+
-
 Mus musculus
1.14.11.2 Fe2+
-
 Homo sapiens
1.14.11.2 Fe2+
-
 Volvox carteri
1.14.11.2 Fe2+ bound: 2 mol/mol Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Gallus gallus the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.2 Gallus gallus
-
-
-
1.14.11.2 Homo sapiens
-
-
-
1.14.11.2 Mus musculus
-
-
-
1.14.11.2 Volvox carteri
-
 green algae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.2 (L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
-
 Gallus gallus (L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 (L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
-
 Gallus gallus (L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 (L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
-
 Homo sapiens (L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 (Pro-Pro-Gly)10 + 2-oxoglutarate + O2
-
 Homo sapiens ? + succinate + CO2
-
 ?
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 (Pro-Pro-Gly)n + 2-oxoglutarate + O2 n: 1,5,10 Mus musculus (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 n: 1,5,10 ?
1.14.11.2 (Pro-Pro-Gly)n + 2-oxoglutarate + O2 n: 1,5,10 Homo sapiens (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 n: 1,5,10 ?
1.14.11.2 2-oxoglutarate + O2 + ascorbate uncoupled oxidative decarboxylation Gallus gallus succinate + dehydroascorbate + CO2 + H2O
-
 ?
1.14.11.2 L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
-
 Gallus gallus L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
-
 Homo sapiens L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain Gallus gallus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 protocollagen type I L-proline + 2-oxoglutarate + O2
-
 Gallus gallus protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 protocollagen type I L-proline+ 2-oxoglutarate + O2
-
 Homo sapiens protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
 r

Subunits

EC Number Subunits Comment Organism
1.14.11.2 monomer the algal enzyme is clearly structurally related to the alpha subunit of the vertebrate enzyme Volvox carteri
1.14.11.2 tetramer characterization of the beta subunit, the beta subunit is a multifunctional polypeptide, having disulfide isomerase activity Homo sapiens
1.14.11.2 tetramer the tetramer appears to contain one active site per pair of dissimilar subunits, the 2-oxoglutarate and peptide binding sites of the enzyme are located on the alpha subunit, whereas the ascorbate binding site may be built up of both alpha and beta subunits Gallus gallus
1.14.11.2 tetramer the tetramer appears to contain one active site per pair of dissimilar subunits, the 2-oxoglutarate and peptide binding sites of the enzyme are located on the alpha subunit, whereas the ascorbate binding site may be built up of both alpha and beta subunits Homo sapiens
1.14.11.2 tetramer there are two forms of the alpha subunit Gallus gallus
1.14.11.2 tetramer there are two forms of the alpha subunit Mus musculus
1.14.11.2 tetramer there are two forms of the alpha subunit Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate
-
 Mus musculus
1.14.11.2 ascorbate
-
 Volvox carteri
1.14.11.2 ascorbate requirement Gallus gallus
1.14.11.2 ascorbate requirement Homo sapiens
1.14.11.2 ascorbate oxygen acceptor in the decarboxylation of 2-oxoglutarate without subsequent hydroxylation of peptide substrate Gallus gallus
1.14.11.2 ascorbate oxygen acceptor in the decarboxylation of 2-oxoglutarate without subsequent hydroxylation of peptide substrate Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.11.2 0.00002
-
 poly (L-proline) molecular weight of 15000 Gallus gallus
1.14.11.2 0.00002
-
 poly (L-proline) molecular weight of 15000 Homo sapiens
1.14.11.2 0.0006
-
 Zn2+
-
 Gallus gallus
1.14.11.2 0.0006
-
 Zn2+
-
 Homo sapiens
1.14.11.2 0.0008
-
 Pyridine-2,5-dicarboxylate
-
 Gallus gallus
1.14.11.2 0.0008
-
 Pyridine-2,5-dicarboxylate
-
 Homo sapiens
1.14.11.2 0.002
-
 Pyridine-2,4-dicarboxylate
-
 Gallus gallus
1.14.11.2 0.002
-
 Pyridine-2,4-dicarboxylate
-
 Homo sapiens
1.14.11.2 0.005
-
 3,4-dihydroxybenzoate competitive inhibitor with respect to ascorbate Gallus gallus