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Information on EC 1.14.11.28 - proline 3-hydroxylase and Organism(s) Homo sapiens and UniProt Accession Q8IVL6

for references in articles please use BRENDA:EC1.14.11.28
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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 .
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Homo sapiens
UNIPROT: Q8IVL6
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Word Map
  • 1.14.11.28
  • 2-oxoglutarate-dependent
  • leprel1
  • early-onset
  • ferrous
  • myopia
  • exome
  • autosomal-recessive
  • choroid
  • neovascularization
  • 3-hydroxyproline
  • regio
  • pharmacology
  • 4-hydroxylase
  • cataract
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
proline 3-hydroxylase, c-p3h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-P3H
-
-
C-P4H
-
-
collagen prolyl hydroxylases 3
-
-
collagen prolyl hydroxylases 4
-
-
Leprel1
prolyl 3-hydroxylase 2
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
162995-24-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P3H3
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
P3H3 can function as a tumour suppressors in breast cancer
physiological function
P3H2 can function as a tumour suppressors in breast cancer
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P3H3_HUMAN
736
0
81837
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G508V
-
mutation is associated with high myopia in human. Mutant G508V expressed in insect cells is completely inactive
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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
-
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 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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
the prolyl 3-hydroxylase P3H3 is a novel targets for epigenetic silencing in breast cancer
pharmacology
the prolyl 3-hydroxylase P3H2 is a novel targets for epigenetic silencing in breast cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team