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Literature summary extracted from

  • Kivirikko, K.I.; Myllylä, R.
    The hydroxylation of prolyl and lysyl residues (1980), Enzymol. Post- transl. Modif. Proteins (Freedman, R. B. , Hawkins, H. C. , eds. ) Academic Press, New York, 1, 53-104.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.11.2 bovine serum albumin activation Gallus gallus
1.14.11.2 bovine serum albumin activation Homo sapiens
1.14.11.2 bovine serum albumin activation Rattus norvegicus
1.14.11.2 catalase activation Gallus gallus
1.14.11.2 catalase activation Homo sapiens
1.14.11.2 catalase activation Rattus norvegicus
1.14.11.2 dithiothreitol activation Gallus gallus
1.14.11.2 dithiothreitol activation Homo sapiens
1.14.11.2 dithiothreitol activation Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 (Gly-Pro-Gly)n competitive inhibitors with respect to the polypeptide substrate Gallus gallus
1.14.11.2 (Gly-Pro-Gly)n competitive inhibitors with respect to the polypeptide substrate Homo sapiens
1.14.11.2 (Pro-Ala-Gly)n competitive inhibitors with respect to the polypeptide substrate Gallus gallus
1.14.11.2 (Pro-Ala-Gly)n competitive inhibitors with respect to the polypeptide substrate Homo sapiens
1.14.11.2 bradykinin analogs especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness Gallus gallus
1.14.11.2 bradykinin analogs especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness Homo sapiens
1.14.11.2 catechol analogues inhibitor of the reaction due in part to the chelation of Fe2+ Gallus gallus
1.14.11.2 catechol analogues inhibitor of the reaction due in part to the chelation of Fe2+ Homo sapiens
1.14.11.2 dilantin inhibitor of the reaction due in part to the chelation of Fe2+ Gallus gallus
1.14.11.2 dilantin inhibitor of the reaction due in part to the chelation of Fe2+ Homo sapiens
1.14.11.2 hydralazine inhibitor of the reaction due in part to the chelation of Fe2+ Gallus gallus
1.14.11.2 hydralazine inhibitor of the reaction due in part to the chelation of Fe2+ Homo sapiens
1.14.11.2 nitroblue tetrazolium is capable of scavenging superoxide, competitive inhibitor with respect to O2 Gallus gallus
1.14.11.2 nitroblue tetrazolium is capable of scavenging superoxide, competitive inhibitor with respect to O2 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 tetracyclin inhibitor of the reaction due in part to the chelation of Fe2+ Gallus gallus
1.14.11.2 tetracyclin inhibitor of the reaction due in part to the chelation of Fe2+ Homo sapiens
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 additional information
-
 additional information effect of amino acids in other parts of the peptide chain, effect of peptide chain length and asymmetry in the hydroxylation of (Pro-Pro-Gly)n Gallus gallus
1.14.11.2 additional information
-
 additional information effect of amino acids in other parts of the peptide chain, effect of peptide chain length and asymmetry in the hydroxylation of (Pro-Pro-Gly)n Homo sapiens
1.14.11.2 0.005
-
 2-oxoglutarate biological substrate Gallus gallus
1.14.11.2 0.022
-
 2-oxoglutarate synthetic substrate Gallus gallus
1.14.11.2 0.043
-
 O2 synthetic substrate Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.2 Fe2+
-
 Homo sapiens
1.14.11.2 Fe2+
-
 Rattus norvegicus
1.14.11.2 Fe2+ Km with biological substrate: 0.002 mM, Km with synthetic substrate: 0.004 mM Gallus gallus
1.14.11.2 Fe2+ very specific requirement, Fe2+ is apparently not firmly bound, the enzyme may bind 4 mol of Fe2+ at its maximum activity, there is a positive co-operativity in this binding, binding may occur to one or more SH-groups Gallus gallus
1.14.11.4 Fe2+
-
 Gallus gallus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.11.2 230000 240000 gel filtration Homo sapiens
1.14.11.2 230000 240000 gel filtration Rattus norvegicus
1.14.11.2 230000 240000 sedimentation equilibrium centrifugation Gallus gallus
1.14.11.4 200000
-
-
 Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.4 collagen + 2-oxoglutarate + O2 Gallus gallus
-
 5-hydroxylysyl-collagen + 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 Rattus norvegicus
-
-
-
1.14.11.4 Gallus gallus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.14.11.2 glycoprotein
-
 Gallus gallus
1.14.11.2 glycoprotein
-
 Homo sapiens
1.14.11.4 glycoprotein
-
 Gallus gallus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.2 using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration Gallus gallus
1.14.11.2 using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration Rattus norvegicus
1.14.11.2 using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration Gallus gallus
1.14.11.2 using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration Homo sapiens
1.14.11.2 using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration Rattus norvegicus
1.14.11.2 using fractionating precipitation, ion-exchange chromatography and gel filtration Gallus gallus
1.14.11.2 using fractionating precipitations, ion-exchange chromatographies and gel filtrations Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 mechanism Gallus gallus
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 mechanism Homo sapiens
a
1.14.11.4 [procollagen]-L-lysine + 2-oxoglutarate + O2 = [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 mechanism Gallus gallus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.2 cartilage embryo Gallus gallus
-
1.14.11.2 embryo tendon cell, cartilage, skin, spleen Gallus gallus
-
1.14.11.2 fetus
-
 Rattus norvegicus
-
1.14.11.2 fetus skin Homo sapiens
-
1.14.11.2 liver
-
 Gallus gallus
-
1.14.11.2 liver
-
 Homo sapiens
-
1.14.11.2 liver
-
 Rattus norvegicus
-
1.14.11.2 skin
-
 Homo sapiens
-
1.14.11.2 skin
-
 Rattus norvegicus
-
1.14.11.2 skin embryo Gallus gallus
-
1.14.11.2 spleen embryo Gallus gallus
-
1.14.11.2 tendon embryo Gallus gallus
-
1.14.11.4 embryo
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.2 proline containing peptide + 2-oxoglutarate + O2
-
 Rattus norvegicus 4-hydroxyproline containing peptide + succinate + CO2
-
 ?
1.14.11.2 proline containing peptide + 2-oxoglutarate + O2 no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation Gallus gallus 4-hydroxyproline containing peptide + succinate + CO2
-
 ?
1.14.11.2 proline containing peptide + 2-oxoglutarate + O2 no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation Homo sapiens 4-hydroxyproline containing peptide + succinate + CO2
-
 ?
1.14.11.2 proline containing peptide + 2-oxoglutarate + O2 the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide Gallus gallus 4-hydroxyproline containing peptide + succinate + CO2
-
 ?
1.14.11.2 proline containing peptide + 2-oxoglutarate + O2 the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide Homo sapiens 4-hydroxyproline containing peptide + succinate + CO2
-
 ?
1.14.11.4 collagen + 2-oxoglutarate + O2
-
 Gallus gallus 5-hydroxylysyl-collagen + succinate + CO2
-
 ?
1.14.11.4 peptidyl-L-lysine + 2-oxoglutarate + O2 minimum sequence required: Xaa-Lys-Gly Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
 ?
1.14.11.4 peptidyl-L-lysine + 2-oxoglutarate + O2 in e.g. lysinevasopressin, lysine-rich histone Gallus gallus peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.2 More structure of the tetramer, physicochemical properties of the subunits Gallus gallus
1.14.11.2 More structure of the tetramer, physicochemical properties of the subunits Homo sapiens
1.14.11.2 tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Gallus gallus
1.14.11.2 tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Homo sapiens
1.14.11.2 tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Rattus norvegicus
1.14.11.4 dimer
-
 Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate requirement Gallus gallus
1.14.11.2 ascorbate requirement Homo sapiens
1.14.11.2 ascorbate requirement Rattus norvegicus
1.14.11.2 ascorbate probably required to prevent oxidation of the enzyme-bound Fe2+ or free enzyme between catalytic cycles, replaceability by certain reduced pteridines and thiols. Km with biological substrate: 0.1 mM, Km with synthetic substrate: 0.3 mM Gallus gallus
1.14.11.2 ascorbate probably required to prevent oxidation of the enzyme-bound Fe2+ or free enzyme between catalytic cycles, replaceability by certain reduced pteridines and thiols. Km with biological substrate: 0.1 mM, Km with synthetic substrate: 0.3 mM Homo sapiens
1.14.11.2 ascorbate pure enzyme, high specificity, dithiothreitol and L-cysteine are the only compounds that give more than 10% of the activity found with the optimal ascorbate concentration, some reduced pteridines give values ranging from 3 to 9% Gallus gallus
1.14.11.4 ascorbate
-
 Gallus gallus