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Information on EC 1.14.11.7 - procollagen-proline 3-dioxygenase
for references in articles please use BRENDA:EC1.14.11.7
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
1.14.11.7 procollagen-proline 3-dioxygenase
IUBMB Comments
Requires Fe2+ and ascorbate. The enzyme forms a complex with protein disulfide isomerase, and is located in the endoplasmic reticulum. It modifies proline residues within the procollagen peptide of certain collagen types. The modification is essential for proper collagen triple helix formation.
The enzyme appears in viruses and cellular organisms
- 1.14.11.7
-
hypoxia-inducible
- fibrosis
- hydroxyproline
- factor-1
- endothelial
- hydroxylases
- hif-1alpha
- erythropoietin
- anemia
-
domain-containing
-
lysyl
- ascorbate
-
oxygen-dependent
-
normoxic
-
hippel-lindau
-
4-hydroxylase
- imperfecta
-
osteogenesis
- dmog
- dimethyloxalylglycine
- bleomycin
- factor-1alpha
-
oxygen-sensing
-
angiogenic
-
2-oxoglutarate-dependent
-
hypoxia-responsive
-
chick-embryo
-
hif-dependent
- hydroxylysine
-
hif-prolyl
-
roxadustat
-
o2-dependent
-
bleomycin-induced
- ppib
- polycythemia
- fkbp10
-
intratracheal
-
3-hydroxylation
-
3,4-dihydroxybenzoic
-
prolyl-hydroxylase
- hepcidin
-
oxygen-sensitive
-
1.14.11.2
-
hydroxyproline-rich
-
col1a2
-
serpinh1
-
lindau
- l-mimosine
-
erythropoiesis-stimulating
Reaction Schemes
show[procollagen]-L-proline
+
+
=
[procollagen]-trans-3-hydroxy-L-proline
+
+
Synonyms
prolyl hydroxylase, lepre1, prolyl 3-hydroxylase, leprel1, prolyl 3-hydroxylase 1, prolyl 3-hydroxylase 2, leprel2, prolyl 3-hydroxylase-2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LEPRE1
Leprel1
oxygenase, protocollagen proline 3-di-
-
-
-
-
P3H1
P3H2
PHD3
proline,2-oxoglutarate 3-dioxygenase
-
-
-
-
prolyl 3-hydroxylase
prolyl 3-hydroxylase 1
prolyl 3-hydroxylase 2
prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen oxidoreductase, 3-hydroxylating
-
-
-
-
protocollagen proline 3-hydroxylase
-
-
-
-
additional information
prolyl 3-hydroxylase
-
-
-
-
additional information
the enzyme belongs to the proline 3-hydroxylase family
additional information
the enzyme belongs to the proline 3-hydroxylase family
additional information
the enzyme belongs to the proline 3-hydroxylase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[procollagen]-L-proline + 2-oxoglutarate + O2 = [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
hydroxylation
-
-
-
-
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
procollagen hydroxylation and glycosylation
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SYSTEMATIC NAME
IUBMB Comments
[procollagen]-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+ and ascorbate. The enzyme forms a complex with protein disulfide isomerase, and is located in the endoplasmic reticulum. It modifies proline residues within the procollagen peptide of certain collagen types. The modification is essential for proper collagen triple helix formation.
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CAS REGISTRY NUMBER
COMMENTARY
63551-75-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(Gly-L-Pro-L-4-hydroxyproline)5 + 2-oxoglutarate + O2
(Gly-trans-3-hydroxy-L-Pro-trans-4-hydrox-L-Pro)5 + succinate + CO2
Substrates: -
Products: -
Products: -
?
(L-Pro-trans-4-hydroxy-L-Pro-Gly)5 + 2-oxoglutarate + O2
(trans-3-hydroxy-L-Pro-trans-4-hydroxy-L-Pro-Gly)5 + succinate + CO2
Substrates: -
Products: -
Products: -
?
L-Leu-L-Asn-Gly-L-Leu-L-4Hyp-Gly-L-Pro-L-Ile-Gly-L-Pro-L-4Hyp-Gly-L-Pro-L-Arg-Gly-L-Arg-L-Thr-Gly-L-Asp-L-Ala-Gly + 2-oxoglutarate + O2
L-Leu-L-Asn-Gly-L-Leu-L-4Hyp-Gly-trans-3-hydroxy-L-Pro-L-Ile-Gly-L-Pro-L-4Hyp-Gly-trans-3-hydroxy-L-Pro-L-Arg-Gly-L-Arg-L-Thr-Gly-L-Asp-L-Ala-Gly + succinate + CO2
Substrates: peptide corresponding to the only prolyl 3-hydroxylation site in the alpha1 chain of collagen I
Products: -
Products: -
?
L-Pro-L-Thr-Gly-L-Pro-L-Arg-Gly-L-Phe-L-Pro-Gly-L-Pro-L-4-hydroxyproline-Gly-L-Pro-L-Asp-Gly-L-Leu-L-4-hydroxyproline-Gly-L-Ser-L-Met-Gly + 2-oxoglutarate + O2
? + succinate + CO2
Substrates: peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
trans 3-hydroxy-L-proline + succinate
-
Substrates: -
Products: -
Products: -
?
L-proline-[collagen] + O2
(S3)-hydroxy-L-proline-[collagen]
Substrates: prolyl 3-hydroxylase 1 modifies a single proline residue in the alpha chains of type I, II, and III collagens to (3S)-hydroxyproline
Products: -
Products: -
?
L-proline-[collagen] + O2
3-hydroxy-L-proline-[collagen]
Substrates: -
Products: -
Products: -
?
L-Ser-L-Lys-Gly-L-Glu-L-Gln-Gly-L-Phe-L-Met-Gly-L-Pro-L-4-hydroxyproline-Gly-L-Pro-L-Gln-Gly-L-Gln-L-4-hydroyproline-Gly-L-Leu-L-4-hydroxyproline-Gly + 2-oxoglutarate + O2
? + succinate + CO2
Substrates: peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
Products: -
Products: -
?
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: proline-labelled polypeptide substrate
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: P3H1 catalyzes the 3-hydroxylation of specific proline residues in procollagen I
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: chicken embryo tendon protocollagen and procollagen or cartilage protocollagen. The formation of 3-hydroxyproline is affected by chain length and the conformation of the substrate, in that longer polypeptide chains proved better substrates, while the native triple-helical conformation of protocollagen or procollagen completely prevents the reaction
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: 2,3-T-L-proline-labeled polypeptide substrate
Products: -
Products: -
?
protocollagen containing 4-hydroxyproline + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
Products: -
?
protocollagen containing 4-hydroxyproline + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: -
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: -
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: prolyl 3-hydroxylation in lens capsule, prolyl 3-hydroxylation at Pro602 from alpha1(IV) and Pro197 from alpha2(IV). Pro707 site in alpha1(I) is a tissue-specific substrate unique to P3h2
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: Residue alpha1(I) K930 is 98% hydroxylated and non-glycosylated in both genotypes and alpha1(I)K87 is 92% hydroxylated in wild-type and 93% in Lepre1H662A/H662A
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: type IV collagen
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: collagen from bovine tissue. 3-hydroxyproline occupancy in collagens from bovine and mouse tissues, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the P3H1-CRTAP-Cyp B complex does not stabilize the collagen triple helix, but does inhibit collgane fibril formation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: the collagen prolyl 3-hydroxylation complex, comprised by cyclophilin B (PPIB), CRTAP and P3H1, catalyzes a specific posttranslational modification of types I, II, and V collagen, and may act as a general chaperone. Collagen 3-hydroxylation complex function, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: P3H1 contains four tetratricopeptide repeats, which are important for protein-protein interactions, and a leucine zipper, L445TREGGPLLYEGISLTMNSKLL466, which is involved in protein dimerization
Products: -
Products: -
?
additional information
?
-
Substrates: type IV collagen contains more prolyl 3-hydroxylation sites than any other collagen types
Products: -
Products: -
?
additional information
?
-
-
Substrates: type IV collagen contains more prolyl 3-hydroxylation sites than any other collagen types
Products: -
Products: -
?
additional information
?
-
-
Substrates: the BH4 domain is required for the interaction of PHD3 with Bcl-2, PHD3 promotes apoptosis via its BH4 domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: results identify a role for P3H2 in 3-hydroxylation of non-A1 proline residues in clade A collagen chains
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-proline-[collagen] + O2
3-hydroxy-L-proline-[collagen]
Substrates: -
Products: -
Products: -
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: P3H1 catalyzes the 3-hydroxylation of specific proline residues in procollagen I
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
Products: -
Products: -
?
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
-
Substrates: the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: -
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: -
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: prolyl 3-hydroxylation in lens capsule, prolyl 3-hydroxylation at Pro602 from alpha1(IV) and Pro197 from alpha2(IV). Pro707 site in alpha1(I) is a tissue-specific substrate unique to P3h2
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: Residue alpha1(I) K930 is 98% hydroxylated and non-glycosylated in both genotypes and alpha1(I)K87 is 92% hydroxylated in wild-type and 93% in Lepre1H662A/H662A
Products: -
Products: -
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
Substrates: type IV collagen
Products: -
Products: -
?
additional information
?
-
Substrates: the P3H1-CRTAP-Cyp B complex does not stabilize the collagen triple helix, but does inhibit collgane fibril formation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform P3H2 is responsible for the hydroxylation of collagen IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: the collagen prolyl 3-hydroxylation complex, comprised by cyclophilin B (PPIB), CRTAP and P3H1, catalyzes a specific posttranslational modification of types I, II, and V collagen, and may act as a general chaperone. Collagen 3-hydroxylation complex function, overview
Products: -
Products: -
?
additional information
?
-
Substrates: type IV collagen contains more prolyl 3-hydroxylation sites than any other collagen types
Products: -
Products: -
?
additional information
?
-
-
Substrates: type IV collagen contains more prolyl 3-hydroxylation sites than any other collagen types
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
L-Leu-L-Asn-Gly-L-Leu-L-4Hyp-Gly-L-Pro-L-Ile-Gly-L-Pro-L-4Hyp-Gly-L-Pro-L-Arg-Gly-L-Arg-L-Thr-Gly-L-Asp-L-Ala-Gly
isoform P3H2, pH 7.8, 37°C
0.07
L-Pro-L-Thr-Gly-L-Pro-L-Arg-Gly-L-Phe-L-Pro-Gly-L-Pro-L-4-hydroxyproline-Gly-L-Pro-L-Asp-Gly-L-Leu-L-4-hydroxyproline-Gly-L-Ser-L-Met-Gly
isoform P3H2, pH 7.8, 37°C
0.26
L-Ser-L-Lys-Gly-L-Glu-L-Gln-Gly-L-Phe-L-Met-Gly-L-Pro-L-4-hydroxyproline-Gly-L-Pro-L-Gln-Gly-L-Gln-L-4-hydroyproline-Gly-L-Leu-L-4-hydroxyproline-Gly
isoform P3H2, pH 7.8, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-oxoadipate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
9.9
2-oxobutyrate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
15
2-oxopentanoate
-
above, competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
2.8
3-oxoglutarate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
1.3
benzene-1,2-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.5
Benzene-1,3-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.5
Benzene-1,4-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
3.1
benzoate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
3.6
Glutarate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
8
laevulinate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
7.4
malonate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.5
oxaloacetate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.7
pyridine-2,3-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.015
Pyridine-2,5-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.2
pyridine-2-carboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
2
pyridine-3,4-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.5
pyridine-3,5-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
4.2
pyruvate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.8
succinate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.003
Pyridine-2,4-dicarboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.3
pyridine-3-carboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.5
pyridine-3-carboxylate
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
quantitation of binding of the P3H1-CRTAP-Cyp B complex to native type I collagen
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
a cell line with myogenic potential derived from embryonic rat heart
brenda
additional information