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1.14.11.2: procollagen-proline 4-dioxygenase

This is an abbreviated version!
For detailed information about procollagen-proline 4-dioxygenase, go to the full flat file.

Word Map on EC 1.14.11.2

Reaction

Procollagen L-proline
+
2-oxoglutarate
+
O2
=
procollagen trans-4-hydroxy-L-proline
+
succinate
+
CO2

Synonyms

A085R, alpha (I) subunit, anthrax-P4H, AT-P4H-1, At-P4H-2, BaP4H, C-P4H, C-P4H alpha subunit (III), C-P4H alpha(I), C-P4H alpha(III), CePHY-1/PHY-2/PDI2, collagen proline hydroxylase, collagen prolyl 4-hydroxylase, collagen prolyl 4-hydroxylase (type-II), collagen prolyl 4-hydroxylase 1, collagen prolyl-4-hydroxylase, collagen prolyl-4-hydroxylase alpha subunit 2, CP4H, CP4H1, CrP4H-1, DmP4H, egg-laying abnormal-9 prolyl hydroxylase, Egl nine homolog, EGLN, EGLN prolyl hydroxylase, EGLN3, EGLN3 hydroxylase, GBAA_4459, HIF prolyl hydroxylase, HIF prolyl-4-hydroxylase, HIF-1alpha-specific prolyl-hydroxylase, HIF-P4H-1, HIF-P4H-2, HIF-P4H-3, HPH, HPH-2, HuPH4-I, HuPH4-II, hydroxylase, collagen proline, hypoxia inducible factor prolyl-4-hydroxylase domain-containing protein, hypoxia inducible factor-prolyl hydroxylase, hypoxia-inducible factor -1alpha-type prolyl 4-hydroxylase, hypoxia-inducible factor prolyl hydroxylase, hypoxia-inducible factor-1alpha-prolyl-hydroxylase 2, More, NtP4H1.1, P4H, P4H alpha1, P4H-1, P4H1, P4ha1, P4ha2, P4Halpha(I), P4Halpha(II), P4Halpha(III), P4Halpha1, PBCV-1 P4H, peptidyl proline hydroxylase, PH, PHD, PHD-1, PHD1, PHD2, PHD3, procollagen prolyl 4-hydroxylase, procollagen-proline dioxygenase, proline 4-hydroxylase, proline hydroxylase, proline protocollagen hydroxylase, proline, 2-oxoglutarate dioxygenase, proline,2-oxoglutarate 4-dioxygenase, prolyl 4-hydroxylase, prolyl 4-hydroxylase A085R, prolyl hydroxylase, prolyl hydroxylase domain 1, prolyl hydroxylase domain containing protein, prolyl hydroxylase domain enzyme, prolyl hydroxylase domain protein 2, prolyl hydroxylase-1, prolyl hydroxylase-3, prolyl-4-hydroxylase, prolyl-4-hydroxylase alpha I, prolyl-4-hydroxylase alpha II, prolyl-4-hydroxylase alpha subunit 2, prolyl-4-hydroxylase alpha1, prolyl-4-hydroxylase-alpha1, prolyl-4-hydroxylases, prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, 4-hydroxylating, prolyl4-hydroxylase, prolylprotocollagen dioxygenase, prolylprotocollagen hydroxylase, protocollagen hydroxylase, protocollagen proline 4-hydroxylase, protocollagen proline dioxygenase, protocollagen proline hydroxylase, protocollagen prolyl hydroxylase, PSB-II, Skp1 prolyl hydroxylase, type I C-P4H, type I proly 4-hydroxylase, type I proyl 4-hydroxylase, type II proyl 4-hydroxylase

ECTree

     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
                1.14.11.2 procollagen-proline 4-dioxygenase

Source Tissue

Source Tissue on EC 1.14.11.2 - procollagen-proline 4-dioxygenase

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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
increase in expression with growth stage, higher expression in muscle than in adipose tissue
Manually annotated by BRENDA team
-
expression is suppressed by tumor necrosis factor TNFalpha via the MKK4-JNK1 pathway, which induces histone 4 lysine 12 acetylation within the TNFalpha response element in the prolyl-4-hydroxylase promoter
Manually annotated by BRENDA team
P4HA2 mRNA levels are significantly upregulated in breast cancer compared to normal mammary tissue
Manually annotated by BRENDA team
-
predominantly type I prolyl-4-hydroxylase
Manually annotated by BRENDA team
-
60 primary colorectal carcinoma tissues, PHD expression analysis, overview. expression of PHD3 is decreased in colorectal cancer, which is associated with higher tumor grade and metastasis, while expression of PHD1 is increased in colorectal tumors. Expression of PHD2 of colorectal tumors is similar to that of paired healthy colorectal tissues
Manually annotated by BRENDA team
-
embryo
Manually annotated by BRENDA team
-
developing
Manually annotated by BRENDA team
-
subcuticular
Manually annotated by BRENDA team
-
embryo, high enzyme activity
Manually annotated by BRENDA team
-
fetus
Manually annotated by BRENDA team
-
a cell line with myogenic potential derived from embryonic rat heart
Manually annotated by BRENDA team
-
treatment with ascorbate in a hypoxic condition for 24 h results in the maximal increase of hydroxyproline by 1.8-fold. The presence of cobalt chloride can substitute for hypoxic condition
Manually annotated by BRENDA team
-
embryo
Manually annotated by BRENDA team
-
embryo, lowest enzyme activity
Manually annotated by BRENDA team
-
a melanoma cell line
Manually annotated by BRENDA team
-
a melanoma cell line
Manually annotated by BRENDA team
-
a melanoma cell line
Manually annotated by BRENDA team
-
derived from primary melanoma
Manually annotated by BRENDA team
-
increase in expression with growth stage, higher expression in muscle than in adipose tissue
Manually annotated by BRENDA team
expression of enzyme alpha-I and alpha-II subunits mRNAs
Manually annotated by BRENDA team
-
a melanoma cell line
Manually annotated by BRENDA team
-
embryo
Manually annotated by BRENDA team
-
type II enzyme represents the main or only enzyme form
Manually annotated by BRENDA team
additional information