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Literature summary for 1.14.11.2 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

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

Application

Application Comment Organism
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)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Drosophila melanogaster
Fe2+ required Chlamydomonas reinhardtii
Fe2+ required Mus musculus
Fe2+ required Rattus norvegicus
Fe2+ required Caenorhabditis elegans
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
procollagen L-proline + 2-oxoglutarate + O2 Drosophila melanogaster
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Chlamydomonas reinhardtii
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Mus musculus
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Rattus norvegicus
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Caenorhabditis elegans
-
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant isozymes Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
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
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
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
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
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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Drosophila melanogaster hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Mus musculus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Homo sapiens hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Rattus norvegicus hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2 i.e. HIF Caenorhabditis elegans hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
?
additional information substrate and ligand binding structures, overview Drosophila melanogaster ?
-
?
additional information substrate and ligand binding structures, overview Chlamydomonas reinhardtii ?
-
?
additional information substrate and ligand binding structures, overview Mus musculus ?
-
?
additional information substrate and ligand binding structures, overview Rattus norvegicus ?
-
?
additional information substrate and ligand binding structures, overview Caenorhabditis elegans ?
-
?
additional information the carboxy group of 2-oxoglutarate is bound by Lys493 in subunit alphaI, substrate and ligand binding structures, overview Homo sapiens ?
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Drosophila melanogaster procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Chlamydomonas reinhardtii procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Mus musculus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Rattus norvegicus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2
-
Caenorhabditis elegans procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Subunits

Subunits Comment Organism
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
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
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
tetramer alpha2beta2 Mus musculus
tetramer alpha2beta2 Rattus norvegicus
tetramer alpha2beta2 formed with three different alpha-subunit isoforms, two of which, alphaI and alphaII, exist both in two splicing variants Homo sapiens

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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]

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

Expression

Organism Comment Expression
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

General Information Comment Organism
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
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
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
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
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
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