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Literature summary extracted from

  • Myllyharju, J.
    Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets (2008), Ann. Med., 40, 402-417.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.11.2 ascorbate required for the decarboxylation reaction step Drosophila melanogaster
1.14.11.2 ascorbate required for the decarboxylation reaction step Chlamydomonas reinhardtii
1.14.11.2 ascorbate required for the decarboxylation reaction step Mus musculus
1.14.11.2 ascorbate required for the decarboxylation reaction step Rattus norvegicus
1.14.11.2 ascorbate required for the decarboxylation reaction step Caenorhabditis elegans

Application

EC Number Application Comment Organism
1.14.11.2 drug development P4H is a target for therapeutic drug development in various pathologies, e.g. angiogenesis, fibrosis, ischemia, anemia, and hypoxia, overview Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.2 recombinant expression of the three isozymes Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.2 P317R naturally occuring mutation, near the Fe2+ binding site, causing erythrocytosis Homo sapiens
1.14.11.2 R371H naturally occuring mutation causing erythrocytosis Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 3,4-dihydroxybenzoic acid
-
 Homo sapiens
1.14.11.2 3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
 Homo sapiens
1.14.11.2 3-hydroxypyridine-2-carbonyl-glycine
-
 Homo sapiens
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Caenorhabditis elegans
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Chlamydomonas reinhardtii
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Drosophila melanogaster
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Homo sapiens
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Mus musculus
1.14.11.2 alpha,alpha'-dipyridyl an Fe2+ chelator Rattus norvegicus
1.14.11.2 Cd2+ competitive versus Fe2+ Caenorhabditis elegans
1.14.11.2 Cd2+ competitive versus Fe2+ Chlamydomonas reinhardtii
1.14.11.2 Cd2+ competitive versus Fe2+ Drosophila melanogaster
1.14.11.2 Cd2+ competitive versus Fe2+ Homo sapiens
1.14.11.2 Cd2+ competitive versus Fe2+ Mus musculus
1.14.11.2 Cd2+ competitive versus Fe2+ Rattus norvegicus
1.14.11.2 ciclopirox olamine an Fe2+ chelator Caenorhabditis elegans
1.14.11.2 ciclopirox olamine an Fe2+ chelator Chlamydomonas reinhardtii
1.14.11.2 ciclopirox olamine an Fe2+ chelator Drosophila melanogaster
1.14.11.2 ciclopirox olamine an Fe2+ chelator Homo sapiens
1.14.11.2 ciclopirox olamine an Fe2+ chelator Mus musculus
1.14.11.2 ciclopirox olamine an Fe2+ chelator Rattus norvegicus
1.14.11.2 Co2+ competitive versus Fe2+ Caenorhabditis elegans
1.14.11.2 Co2+ competitive versus Fe2+ Chlamydomonas reinhardtii
1.14.11.2 Co2+ competitive versus Fe2+ Drosophila melanogaster
1.14.11.2 Co2+ competitive versus Fe2+ Homo sapiens
1.14.11.2 Co2+ competitive versus Fe2+ Mus musculus
1.14.11.2 Co2+ competitive versus Fe2+ Rattus norvegicus
1.14.11.2 desferrioxamine an Fe2+ chelator Caenorhabditis elegans
1.14.11.2 desferrioxamine an Fe2+ chelator Chlamydomonas reinhardtii
1.14.11.2 desferrioxamine an Fe2+ chelator Drosophila melanogaster
1.14.11.2 desferrioxamine an Fe2+ chelator Homo sapiens
1.14.11.2 desferrioxamine an Fe2+ chelator Mus musculus
1.14.11.2 desferrioxamine an Fe2+ chelator Rattus norvegicus
1.14.11.2 fumarate
-
 Homo sapiens
1.14.11.2 N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
-
 Homo sapiens
1.14.11.2 Ni2+ competitive versus Fe2+ Caenorhabditis elegans
1.14.11.2 Ni2+ competitive versus Fe2+ Chlamydomonas reinhardtii
1.14.11.2 Ni2+ competitive versus Fe2+ Drosophila melanogaster
1.14.11.2 Ni2+ competitive versus Fe2+ Homo sapiens
1.14.11.2 Ni2+ competitive versus Fe2+ Mus musculus
1.14.11.2 Ni2+ competitive versus Fe2+ Rattus norvegicus
1.14.11.2 oxalylglycine
-
 Homo sapiens
1.14.11.2 Pyridine 2,4-dicarboxylate
-
 Homo sapiens
1.14.11.2 Pyridine 2,5-dicarboxylate
-
 Homo sapiens
1.14.11.2 succinate product inhibition Homo sapiens
1.14.11.2 Zn2+ competitive versus Fe2+ Caenorhabditis elegans
1.14.11.2 Zn2+ comptitive versus Fe2+ Chlamydomonas reinhardtii
1.14.11.2 Zn2+ competitive versus Fe2+ Drosophila melanogaster
1.14.11.2 Zn2+ competitive versus Fe2+ Homo sapiens
1.14.11.2 Zn2+ competitive versus Fe2+ Mus musculus
1.14.11.2 Zn2+ competitive versus Fe2+ Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.2 0.001
-
 2-oxoglutarate with substrate HIF, isozyme P4H-II Homo sapiens
1.14.11.2 0.002
-
 2-oxoglutarate with substrate HIF, isozyme P4H-I Homo sapiens
1.14.11.2 0.012
-
 2-oxoglutarate with substrate HIF, isozyme P4H-III Homo sapiens
1.14.11.2 0.02
-
 2-oxoglutarate with substrate procollagen, isozymes P4H-I and P4H-III Homo sapiens
1.14.11.2 0.022
-
 2-oxoglutarate with substrate procollagen, isozyme P4H-II Homo sapiens
1.14.11.2 0.04
-
 O2 with substrate procollagen, isozyme P4H-I Homo sapiens
1.14.11.2 0.065 0.25 O2 with substrate HIF at different fragment lengths, isozyme P4H-II Homo sapiens
1.14.11.2 0.23
-
 O2 with substrate HIF, isozymes P4H-I and P4H-III Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.2 endoplasmic reticulum lumen
-
 Mus musculus 5788
-
1.14.11.2 endoplasmic reticulum lumen
-
 Homo sapiens 5788
-
1.14.11.2 endoplasmic reticulum lumen
-
 Rattus norvegicus 5788
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.2 Fe2+ required Drosophila melanogaster
1.14.11.2 Fe2+ required Chlamydomonas reinhardtii
1.14.11.2 Fe2+ required Mus musculus
1.14.11.2 Fe2+ required Rattus norvegicus
1.14.11.2 Fe2+ required Caenorhabditis elegans
1.14.11.2 Fe2+ required, bound by residues His412, Asp414, and His483. KM with procollagen is 0.002 mM for isozymes P4H-I and P4H-II, and 0.0005 for isozyme P4H-III Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 Drosophila melanogaster i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 Mus musculus i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 Caenorhabditis elegans i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 Homo sapiens i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 Rattus norvegicus i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Drosophila melanogaster
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Chlamydomonas reinhardtii
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Mus musculus
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Rattus norvegicus
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 Caenorhabditis elegans
-
 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.2 Caenorhabditis elegans
-
 4 isozymes
-
1.14.11.2 Chlamydomonas reinhardtii
-
-
-
1.14.11.2 Drosophila melanogaster
-
 at least 19 isozymes
-
1.14.11.2 Homo sapiens
-
 isozymes P4H-I, P4H-II and P4H-III, or P4H-1, P4H-2 and P4H-3
-
1.14.11.2 Mus musculus
-
-
-
1.14.11.2 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.2 recombinant isozymes Homo sapiens

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 reaction mechanism involving ascorbate, which are not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Mus musculus
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism involving ascorbate, which not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Drosophila melanogaster
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism involving ascorbate, which not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Chlamydomonas reinhardtii
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism involving ascorbate, which not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Homo sapiens
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism involving ascorbate, which not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Rattus norvegicus
a
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 reaction mechanism involving ascorbate, which not required for the hydroxylation reaction part, but for the uncoupled cedarboxylation, overview Caenorhabditis elegans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview Drosophila melanogaster hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview Mus musculus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview Caenorhabditis elegans hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview Homo sapiens hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview Rattus norvegicus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Drosophila melanogaster hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Mus musculus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Homo sapiens hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Rattus norvegicus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Caenorhabditis elegans hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 additional information substrate and ligand binding structures, overview Drosophila melanogaster ?
-
 ?
1.14.11.2 additional information substrate and ligand binding structures, overview Chlamydomonas reinhardtii ?
-
 ?
1.14.11.2 additional information substrate and ligand binding structures, overview Mus musculus ?
-
 ?
1.14.11.2 additional information substrate and ligand binding structures, overview Rattus norvegicus ?
-
 ?
1.14.11.2 additional information substrate and ligand binding structures, overview Caenorhabditis elegans ?
-
 ?
1.14.11.2 additional information the carboxy group of 2-oxoglutarate is bound by Lys493 in subunit alphaI, substrate and ligand binding structures, overview Homo sapiens ?
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Drosophila melanogaster procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Chlamydomonas reinhardtii procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Mus musculus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Rattus norvegicus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?
1.14.11.2 procollagen L-proline + 2-oxoglutarate + O2
-
 Caenorhabditis elegans procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.2 More the beta-subunit is identical to the beta-subunit of the chaperone protein disulfide isomerase, EC 5.3.4.1. The beta-subunit is responsible for keeping the catalytic alpha-subunit active, in non-aggregated conformation and for retaining the enzyme within the lumen of the endoplasmic reticulum via its C-terminal retention signal Mus musculus
1.14.11.2 More the beta-subunit is identical to the beta-subunit of the chaperone protein disulfide isomerase, EC 5.3.4.1. The beta-subunit is responsible for keeping the catalytic alpha-subunit active, in non-aggregated conformation and for retaining the enzyme within the lumen of the endoplasmic reticulum via its C-terminal retention signal Homo sapiens
1.14.11.2 More the beta-subunit is identical to the beta-subunit of the chaperone protein disulfide isomerase, EC 5.3.4.1. The beta-subunit is responsible for keeping the catalytic alpha-subunit active, in non-aggregated conformation and for retaining the enzyme within the lumen of the endoplasmic reticulum via its C-terminal retention signal Rattus norvegicus
1.14.11.2 tetramer alpha2beta2 Mus musculus
1.14.11.2 tetramer alpha2beta2 Rattus norvegicus
1.14.11.2 tetramer alpha2beta2 formed with three different alpha-subunit isoforms, two of which, alphaI and alphaII, exist both in two splicing variants Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Drosophila melanogaster
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Chlamydomonas reinhardtii
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Mus musculus
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Homo sapiens
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Rattus norvegicus
1.14.11.2 More the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases Caenorhabditis elegans
1.14.11.2 P4H
-
 Drosophila melanogaster
1.14.11.2 P4H
-
 Chlamydomonas reinhardtii
1.14.11.2 P4H
-
 Mus musculus
1.14.11.2 P4H
-
 Homo sapiens
1.14.11.2 P4H
-
 Rattus norvegicus
1.14.11.2 P4H
-
 Caenorhabditis elegans
1.14.11.2 prolyl 4-hydroxylase
-
 Drosophila melanogaster
1.14.11.2 prolyl 4-hydroxylase
-
 Chlamydomonas reinhardtii
1.14.11.2 prolyl 4-hydroxylase
-
 Mus musculus
1.14.11.2 prolyl 4-hydroxylase
-
 Homo sapiens
1.14.11.2 prolyl 4-hydroxylase
-
 Rattus norvegicus
1.14.11.2 prolyl 4-hydroxylase
-
 Caenorhabditis elegans

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate required for the decarboxylation reaction step, KM with procollagen is 0.30 mM for isozyme P4H-I, 0.34 for isozyme P4H-II, and 0.37 for isozyme P4H-III. KM with HIF is 0.17 mM for isozyme P4H-I, 0.18 for isozyme P4H-II, and 0.14 for isozyme P4H-III Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.11.2 0.00006
-
 N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.0002
-
 N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine isozymes P4H-II and P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.0004
-
 3-hydroxypyridine-2-carbonyl-glycine isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.0008
-
 N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.0008
-
 Pyridine 2,5-dicarboxylate isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.001
-
 3-hydroxypyridine-2-carbonyl-glycine isozyme P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.0019
-
 oxalylglycine isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.002
-
 Pyridine 2,4-dicarboxylate isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.002
-
 3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.002
-
 3-hydroxypyridine-2-carbonyl-glycine isozyme P4H-II, with substrate HIF Homo sapiens
1.14.11.2 0.005
-
 3,4-dihydroxybenzoic acid isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.007
-
 Pyridine 2,4-dicarboxylate isozyme P4H-II, with substrate HIF Homo sapiens
1.14.11.2 0.008
-
 oxalylglycine isozyme P4H-II, with substrate HIF Homo sapiens
1.14.11.2 0.008
-
 Pyridine 2,4-dicarboxylate isozyme P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.01
-
 oxalylglycine isozyme P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.01
-
 3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline isozymes P4H-II and P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.015
-
 3-hydroxypyridine-2-carbonyl-glycine isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.03
-
 3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.04
-
 Pyridine 2,4-dicarboxylate isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.05
-
 oxalylglycine isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.05
-
 fumarate isozyme P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.06
-
 fumarate isozyme P4H-II, with substrate HIF Homo sapiens
1.14.11.2 0.08
-
 fumarate isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.19
-
 fumarate isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.3
-
 Pyridine 2,5-dicarboxylate above, isozymes P4H-I-III, with substrate HIF Homo sapiens
1.14.11.2 0.3
-
 3,4-dihydroxybenzoic acid isozymes P4H-I-III, with substrate HIF Homo sapiens
1.14.11.2 0.35
-
 succinate isozyme P4H-I, with substrate HIF Homo sapiens
1.14.11.2 0.4
-
 succinate isozyme P4H-I, with substrate procollagen Homo sapiens
1.14.11.2 0.43
-
 succinate isozyme P4H-III, with substrate HIF Homo sapiens
1.14.11.2 0.46
-
 succinate isozyme P4H-II, with substrate HIF Homo sapiens

Expression

EC Number Organism Comment Expression
1.14.11.2 Mus musculus P4H alphaII or alphaIII null mice with 20% of wild-type enzyme activity do not show an abnormal phenotype, while P4H alpha I null mutants die at day E10.5 and show an overall developmental delay and rupture of the basement membranes due to a lack of collgane IV, overview down

General Information

EC Number General Information Comment Organism
1.14.11.2 malfunction excessive collagen formation is involved in the pathogenesis of fibrosis, e.g. in liver and lung, resulting in abnormal wound healing and deformed tissue architecture Homo sapiens
1.14.11.2 physiological function 4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in a single isozyme form Drosophila melanogaster
1.14.11.2 physiological function 4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in a single isozyme form Caenorhabditis elegans
1.14.11.2 physiological function 4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in three different isozyme forms Mus musculus
1.14.11.2 physiological function 4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in three different isozyme forms Homo sapiens
1.14.11.2 physiological function 4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in three different isozyme forms Rattus norvegicus