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Information on EC 1.14.11.28 - proline 3-hydroxylase
for references in articles please use BRENDA:EC1.14.11.28
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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
1.14.11.28 proline 3-hydroxylase
IUBMB Comments
Requires iron(II) for activity. Unlike the proline hydroxylases involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)], this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme . The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.11.28
-
2-oxoglutarate-dependent
- leprel1
-
early-onset
-
ferrous
- myopia
-
exome
-
autosomal-recessive
-
choroid
-
neovascularization
-
3-hydroxyproline
-
regio
- pharmacology
-
4-hydroxylase
-
cataract
showSynonyms
proline 3-hydroxylase, c-p3h, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-proline-3-hydroxylase
Leprel1
P-3-H
P3H
P3H2
proline 3-hydroxylase
proline 3-hydroxylase type I
proline 3-hydroxylase type II
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires iron(II) for activity. Unlike the proline hydroxylases involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)], this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme [2]. The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates [2].
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CAS REGISTRY NUMBER
COMMENTARY
162995-24-6
-
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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
L-2-azetidinecarboxylic acid + 2-oxoglutarate + O2
cis-3-hydroxyazetidine-L-2-carboxylic acid + succinate + CO2
3,4-dehydro-L-proline + 2-oxoglutarate + O2
cis-3,4-epoxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
3,4-dehydro-L-proline + 2-oxoglutarate + O2
cis-3,4-epoxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-2-azetidinecarboxylic acid + 2-oxoglutarate + O2
cis-3-hydroxyazetidine-L-2-carboxylic acid + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-2-azetidinecarboxylic acid + 2-oxoglutarate + O2
cis-3-hydroxyazetidine-L-2-carboxylic acid + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-pipecolic acid + 2-oxoglutarate + O2
cis-3-hydroxy-L-pipecolic acid + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-pipecolic acid + 2-oxoglutarate + O2
cis-3-hydroxy-L-pipecolic acid + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: product identification and analysis by NMR spectroscopy
Products: product identification and analysis by NMR spectroscopy
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: product identification and analysis by NMR spectroscopy
Products: product identification and analysis by NMR spectroscopy
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
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 + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-proline + 2-oxoglutarate + O2
cis-3-hydroxy-L-proline + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
1 mM added to cell extracts, 60% inhibition without addition of Fe2+
Fe2+
-
1 mM added to cell extracts, 85% inhibition without addition of Fe2+
Fe2+
-
1 mM added to cell extracts, complete inhibition without addition of Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoCl2
-
82% inhibition at 0.1 mM, 98% inhibition at 1 mM, 5 mM 2-oxoglutarate, 1 mM ferrous sulfate, 5 mM L-ascorbic acid, 100 mM TES pH 7.5, 30°C
CuSO4
-
59% inhibition at 0.1 mM, complete inhibition at 1 mM, 5 mM 2-oxoglutarate, 1 mM ferrous sulfate, 5 mM L-ascorbic acid, 100 mM TES pH 7.5, 30°C
ZnSO4
-
95% inhibition at 0.1 mM, complete inhibition at 1 mM, 5 mM 2-oxoglutarate, 1 mM ferrous sulfate, 5 mM L-ascorbic acid, 100 mM TES pH 7.5, 30°C
EDTA
-
95% inhibition at 2 mM, 5 mM 2-oxoglutarate, 1 mM ferrous sulfate, 5 mM L-ascorbic acid, 100 mM TES pH 7.5, 30°C
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Lymphoma
The collagen prolyl hydroxylases are novel transcriptionally silenced genes in lymphoma.
Neoplasms
The collagen prolyl hydroxylases are novel transcriptionally silenced genes in lymphoma.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
2-oxoglutarate
-
100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C
0.56
L-proline
-
100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
L-proline
-
100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00119
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5 mM 2-oxoglutarate, 1 mM ferrous sulfate, 5 mM L-ascorbic acid, 100 mM TES pH 7.5, 30°C
additional information
-
recombinant biotransformation of L-proline to cis-3-hydroxy-L-proline in Escherichia coli cells transformed with a synthetic P3H gene, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
P3H2 can function as a tumour suppressors in breast cancer
physiological function
P3H3 can function as a tumour suppressors in breast cancer
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G508V
-
mutation is associated with high myopia in human. Mutant G508V expressed in insect cells is completely inactive
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene P3H, DNA and amino acid sequence determination and analysis, preparation of a synthetic gene encoding proline 3-hydroxylase and cloning and overexpression of proline 3-hydroxylase protein in Escherichia coli strain BL21(DE3) resulting in strain SC16497, biotransformation rates, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
C-P3H is downregulated in lymphoma. Down-regulation is associated with methylation in the CpG islands and is detected in almost all common types of B-cell lymphoma
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C-P4H is downregulated in lymphoma. Down-regulation is associated with methylation in the CpG islands and is detected in almost all common types of B-cell lymphoma
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the enzyme expression of P3H2 and P3H3 is downregulated in breast cancer by abberrant CpG methylation in the 5'-regulatory sequences of each gene, methylation of P3H3 is not associated with higher tumour grade and Nottingham prognostic index
the enzyme expression of P3H2 is downregulated in breast cancer by abberrant CpG methylation in the 5'-regulatory sequences of each gene, methylation of P3H2 is specific for breast cancer and does not occur in other cancer cell types, it is strongly associated with higher tumour grade and Nottingham prognostic index
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
pharmacology
the prolyl 3-hydroxylase P3H2 is a novel targets for epigenetic silencing in breast cancer
pharmacology
the prolyl 3-hydroxylase P3H3 is a novel targets for epigenetic silencing in breast cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, H.; Shibasaki, T.; Uozaki, Y.; Ochiai, K.; Ozaki, A.
Detection of novel proline 3-hydroxylase activities in Streptomyces and Bacillus spp. by regio- and stereospecific hydroxylation of L-proline
Appl. Environ. Microbiol.
62
1903-1907
1996
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) TH2, Bacillus sp. (in: Bacteria) TH3, Streptomyces canus, Streptomyces sp., Streptomyces sp. TH1
brenda
Shibasaki, T.; Mori, H.; Ozaki, A.
Cloning of an isozyme of proline 3-hydroxylase and its purification from recombinant Escherichia coli
Biotechnol. Lett.
22
1967-1973
2000
Streptomyces sp., Streptomyces sp. TH1
-
brenda
Clifton, I.J.; Hsueh, L.C.; Baldwin, J.E.; Harlos, K.; Schofield, C.J.
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases
Eur. J. Biochem.
268
6625-6636
2001
Streptomyces sp., Streptomyces sp. TH1
brenda
Mori, H.; Shibasaki, T.; Yano, K.; Ozaki, A.
Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline
J. Bacteriol.
179
5677-5683
1997
Streptomyces sp., Streptomyces sp. TH1
brenda
Vranka, J.A.; Sakai, L.Y.; Bachinger, H.P.
Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
J. Biol. Chem.
279
23615-23621
2004
Gallus gallus
brenda
Shibasaki, T.; Sakurai, W.; Hasegawa, A.; Uosaki, Y.; Mori, H.; Yoshida, M.; Ozaki, A.
Substrate selectivities of proline hydroxylases
Tetrahedron Lett.
40
5227-5230
1999
Streptomyces sp., Streptomyces sp. TH1
-
brenda
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 (Q32P28), Homo sapiens (Q8IVL6)
brenda
Johnston, R.; Chu, L.; Liu, M.; Goldberg, S.; Goswami, A.; Patel, R.
Hydroxylation of L-proline to cis-3-hydroxy-L-proline by recombinant Escherichia coli expressing a synthetic L-proline-3-hydroxylase gene
Enzyme Microb. Technol.
45
484-490
2009
Streptomyces sp., Streptomyces sp. TH1
-
brenda
Mordechai, S.; Gradstein, L.; Pasanen, A.; Ofir, R.; El Amour, K.; Levy, J.; Belfair, N.; Lifshitz, T.; Joshua, S.; Narkis, G.; Elbedour, K.; Myllyharju, J.; Birk, O.S.
High myopia caused by a mutation in LEPREL1, encoding prolyl 3-hydroxylase 2
Am. J. Hum. Genet.
89
438-445
2011
Homo sapiens
brenda
Hatzimichael, E.; Lo Nigro, C.; Lattanzio, L.; Syed, N.; Shah, R.; Dasoula, A.; Janczar, K.; Vivenza, D.; Monteverde, M.; Merlano, M.; Papoudou-Bai, A.; Bai, M.; Schmid, P.; Stebbing, J.; Bower, M.; Dyer, M.J.; Karran, L.E.; ElguetaKarstegl, C.; Farrell, P.J.; Thompson, A.; Briasoulis, E.; Crook, T.
The collagen prolyl hydroxylases are novel transcriptionally silenced genes in lymphoma
Br. J. Cancer
107
1423-1432
2012
Homo sapiens
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.11.28)
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