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Information on EC 1.14.11.7 - procollagen-proline 3-dioxygenase and Organism(s) Gallus gallus and UniProt Accession Q6JHU8

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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:
Gallus gallus
UNIPROT: Q6JHU8
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The taxonomic range for the selected organisms is: Gallus gallus
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 1
-
oxygenase, protocollagen proline 3-di-
-
-
-
-
proline,2-oxoglutarate 3-dioxygenase
-
-
-
-
prolyl 3-hydroxylase
-
-
-
-
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
L-proline-[collagen] + O2
(S3)-hydroxy-L-proline-[collagen]
show the reaction diagram
prolyl 3-hydroxylase 1 modifies a single proline residue in the alpha chains of type I, II, and III collagens to (3S)-hydroxyproline
-
-
?
procollagen + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
proline-labelled polypeptide substrate
-
-
?
protocollagen containing 4-hydroxyproline + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
the P3H1-CRTAP-Cyp B complex does not stabilize the collagen triple helix, but does inhibit collgane fibril formation, overview
-
-
?
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 + 2-oxoglutarate + O2
procollagen trans-3-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues
-
-
?
additional information
?
-
the P3H1-CRTAP-Cyp B complex does not stabilize the collagen triple helix, but does inhibit collgane fibril formation, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoadipate
-
-
2-oxobutyrate
-
-
2-oxpentanoate
-
-
3-oxoglutarate
-
-
adipate
-
-
benzene-1,2-dicarboxylate
-
-
Benzene-1,3-dicarboxylate
-
-
Benzene-1,4-dicarboxylate
-
-
benzoate
-
-
concanavalin A
-
-
-
Glutarate
-
-
laevulinate
-
-
malonate
-
-
oxaloacetate
-
-
pyridine-2,3-dicarboxylate
-
-
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
-
-
pyridine-2-carboxylate
-
-
pyridine-3,4-dicarboxylate
-
-
pyridine-3,5-dicarboxylate
-
-
pyridine-3-carboxylate
-
-
pyridine-4-carboxylate
-
-
pyruvate
-
-
succinate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
2-oxoglutarate
-
-
0.03
O2
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
6
adipate
-
-
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
0.003
Pyridine-2,4-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
0.3 - 0.5
pyridine-3-carboxylate
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is organized in an enzyme complex formed by prolyl3-hydroxylase 1, cartilage-associated protein, and cyclophilin B
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P3H1_CHICK
725
0
81676
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native prolyl 3-hydroxylation complex from embrtyos by ultracentrifugation and gelatin affinity chromatography
partial
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latip, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.
Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate
Biochem. J.
229
127-133
1985
Gallus gallus
Manually annotated by BRENDA team
Tryggvason, K.; Majamaa, K.; Risteli, J.; Kivirikko, K.I.
Partial purification and characterization of chick-embryo prolyl 3-hydroxylase
Biochem. J.
183
303-307
1979
Gallus gallus
Manually annotated by BRENDA team
Ishikawa, Y.; Wirz, J.; Vranka, J.A.; Nagata, K.; Baechinger, H.P.
Biochemical characterization of the prolyl 3-hydroxylase 1 cartilage-associated protein cyclophilin B complex
J. Biol. Chem.
284
17641-17647
2009
Gallus gallus (Q6JHU8)
Manually annotated by BRENDA team