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Information on EC 1.14.11.7 - procollagen-proline 3-dioxygenase and Organism(s) Homo sapiens and UniProt Accession Q8IVL5

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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.
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This record set is specific for:
Homo sapiens
UNIPROT: Q8IVL5
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[procollagen]-L-proline
+
2-oxoglutarate
+
O2
=
[procollagen]-trans-3-hydroxy-L-proline
+
succinate
+
CO2
[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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
prolyl 3-hydroxylase
-
prolyl 3-hydroxylase 2
-
LEPRE1
oxygenase, protocollagen proline 3-di-
-
-
-
-
PHD3
-
-
proline,2-oxoglutarate 3-dioxygenase
-
-
-
-
prolyl 3-hydroxylase
prolyl 3-hydroxylase 1
prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen oxidoreductase, 3-hydroxylating
-
-
-
-
protocollagen proline 3-hydroxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
redox reaction
-
-
-
-
hydroxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
63551-75-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
?
(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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
peptide corresponding to the only prolyl 3-hydroxylation site in the alpha1 chain of collagen I
-
-
?
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
show the reaction diagram
peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
-
-
?
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
show the reaction diagram
peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
-
-
?
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
?
(Gly-L-Pro-L-4-hydroxyproline)5 + 2-oxoglutarate + O2
(Gly-trans-3-hydroxy-L-Pro-trans-4-hydrox-L-Pro)5 + succinate + CO2
show the reaction diagram
-
-
-
?
(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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
peptide corresponding to the only prolyl 3-hydroxylation site in the alpha1 chain of collagen I
-
-
?
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
show the reaction diagram
peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
-
-
?
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
show the reaction diagram
peptide corresponding to a known prolyl 3-hydroxylation site in the alpha1 chain of collagen IV
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[procollagen]-L-proline + 2-oxoglutarate + O2
[procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
Km value 0.11 mM
ascorbate
Km value 0.11 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
Km value 0.0005 mM
Fe2+
Km value 0.0005 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
poly(L-Pro)
MW 7000-8000 Da
Pyridine-2,4-dicarboxylate
-
Pyridine-2,5-dicarboxylate
-
poly(L-Pro)
MW 7000-8000 Da
Pyridine-2,4-dicarboxylate
-
Pyridine-2,5-dicarboxylate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(Gly-L-Pro-L-4-hydroxyproline)5
isoform P3H2, pH 7.8, 37°C
0.08
2-oxoglutarate
isoform P3H2, pH 7.8, 37°C
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
0.07
(Gly-L-Pro-L-4-hydroxyproline)5
isoform P3H2, pH 7.8, 37°C
0.08
2-oxoglutarate
isoform P3H2, pH 7.8, 37°C
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
poly(L-Pro)
isoform P3H2, pH 7.8, 37°C
0.009 - 1
Pyridine-2,4-dicarboxylate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
collagen 3-hydroxylase complex
Manually annotated by BRENDA team
additional information
-
P3H1 contains transmembrane sequences Ala5-Val33 and Glu372-Phe387, but is not associated with membranes
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
the enzyme could be considered as a potential target for anti-angiogenesis therapy
malfunction
epigenetic inactivation of the enzyme in human cancer
physiological function
malfunction
physiological function
the enzyme acts as a tumor suppressor
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P3H2_HUMAN
708
0
80984
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme contains two potential myristoylation sequences G53VVLSM58 and G667QRCAI672 and 20 potential recognition sites for phosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
most of the recombinant isoform P3H2 is insoluble. Coexpression of protein with the cartilage-associated protein CRTAP does not enhance solubility
most of the recombinant isoform P3H2 is insoluble. Coexpression of protein with the cartilage-associated protein CRTAP does not enhance solubility
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ectopic expression of P3H2 in cells with silenced endogenous genes
expression of both isoforms P3H1, P3H2 in Sf9 cell
DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
-
ectopic expression of P3H3 in cells with silenced endogenous genes
expression of both isoforms P3H1, P3H2 in Sf9 cell
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of P3H2 , or Leprel1, but not of P3H1 or Leprecan, is specifically downregulated in breast cancer by abberrant CpG methylation in the 5' regulatory sequences of the genes. Methylation of P3H2 is strongly associated with estrogen-receptor-positive breast cancers
the expression of P3H3, or Leprel2, but not of P3H1 or Leprecan, is specifically downregulated in breast cancer by abberrant CpG methylation in the 5' regulatory sequences of the genes. Methylation of P3H3 is not associated with estrogen-receptor-positive breast cancers, while P3H3 isassociated with higher tumour grade and Nottingham prognostic index
TNF-alpha and IL-1beta robustly increase PHD3 expression in an NF-kappaB dependent fashion
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tiainen, P.; Pasanen, A.; Sormunen, R.; Myllyharju, J.
Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV
J. Biol. Chem.
283
19432-19439
2008
Homo sapiens (Q32P28), Homo sapiens (Q8IVL5), Homo sapiens
Manually annotated by BRENDA team
Shah, R.; Smith, P.; Purdie, C.; Quinlan, P.; Baker, L.; Aman, P.; Thompson, A.M.; Crook, T.
The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer
Br. J. Cancer
100
1687-1696
2009
Homo sapiens (Q8IVL5), Homo sapiens (Q8IVL6)
Manually annotated by BRENDA team
Marini, J.C.; Cabral, W.A.; Barnes, A.M.
Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta
Cell Tissue Res.
339
59-70
2009
Homo sapiens
Manually annotated by BRENDA team
Chang, W.; Barnes, A.M.; Cabral, W.A.; Bodurtha, J.N.; Marini, J.C.
Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex
Hum. Mol. Genet.
19
223-234
2009
Homo sapiens (Q32P28), Homo sapiens
Manually annotated by BRENDA team
Fujita, N.; Gogate, S.S.; Chiba, K.; Toyama, Y.; Shapiro, I.M.; Risbud, M.V.
Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-alpha (TNF-alpha) on cells of the nucleus pulposus through co-activation of nuclear factor kappaB (NF-kappaB)/p65 signaling
J. Biol. Chem.
287
39942-39953
2012
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Pignata, P.; Apicella, I.; Cicatiello, V.; Puglisi, C.; Magliacane Trotta, S.; Sanges, R.; Tarallo, V.; De Falco, S.
Prolyl 3-hydroxylase 2 is a molecular player of angiogenesis
Int. J. Mol. Sci.
22
3896
2021
Mus musculus (Q8CG71), Homo sapiens (Q8IVL5), Homo sapiens
Manually annotated by BRENDA team