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Literature summary for 1.14.11.2 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
Search for more literature for 1.14.11.2

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
(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
(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
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
-
 Homo sapiens ? + succinate + CO2
-
 ?
(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 ?
(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 ?
(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 ?
2-oxoglutarate + O2 + ascorbate uncoupled oxidative decarboxylation Gallus gallus succinate + dehydroascorbate + CO2 + H2O
-
 ?
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
-
 Gallus gallus L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
-
 Homo sapiens L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
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
-
 ?
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
-
 ?
protocollagen type I L-proline + 2-oxoglutarate + O2
-
 Gallus gallus protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
protocollagen type I L-proline+ 2-oxoglutarate + O2
-
 Homo sapiens protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
 r

Subunits

Subunits Comment Organism
monomer the algal enzyme is clearly structurally related to the alpha subunit of the vertebrate enzyme Volvox carteri
tetramer characterization of the beta subunit, the beta subunit is a multifunctional polypeptide, having disulfide isomerase activity Homo sapiens
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
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
tetramer there are two forms of the alpha subunit Gallus gallus
tetramer there are two forms of the alpha subunit Mus musculus
tetramer there are two forms of the alpha subunit Homo sapiens

Cofactor

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

Ki Value [mM]

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