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Literature summary for 1.14.11.2 extracted from

  • Guzman, N.A.; Ascari, W.Q.; Cutroneo, K.R.; Desnick, R.J.
    Comparison between avian and human prolyl 4-hydroxylases: studies on the holomeric enzymes and their constituent subunits (1992), J. Cell. Biochem., 48, 172-189.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
bleomycin activation Gallus gallus
bleomycin activation Homo sapiens
bovine serum albumin activation Gallus gallus
bovine serum albumin activation Homo sapiens
catalase activation Gallus gallus
catalase activation Homo sapiens
Chelating agents activation Gallus gallus
Chelating agents activation Homo sapiens
dithiothreitol activation Gallus gallus
dithiothreitol activation Homo sapiens
nucleoside triphosphates stimulate Gallus gallus
nucleoside triphosphates stimulate Homo sapiens
Thymol activation Gallus gallus
Thymol activation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2,2'-dipyridyl
-
Gallus gallus
2,2'-dipyridyl
-
Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum luminal site Gallus gallus 5783
-
endoplasmic reticulum luminal site Homo sapiens 5783
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Gallus gallus
Fe2+ purified enzyme does not require exogenous Fe2+ to obtain full enzymic activity, the iron in the holomeric placental enzyme appears to be more tightly bound than in the chick embryo enzyme Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
400000 600000 value depending on salt concentration of buffer Gallus gallus
400000 600000 value depending on salt concentration of buffer Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2 Gallus gallus key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 Homo sapiens key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein carbohydrate composition Gallus gallus
glycoprotein carbohydrate composition Homo sapiens
glycoprotein 29.8 residues mannose and 3.8 residues N-acetyl-glucosamine per 240 kDa Homo sapiens
glycoprotein 35.4 residues mannose and 3.9 residues N-acetyl-glucosamine per 240 kDa Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
using chromatography on DEAE-cellulose column, affinity column, anion-exchange chromatography and a second chromatography on DEAE-cellulose column Gallus gallus
using chromatography on DEAE-cellulose column, affinity column, anion-exchange chromatography and a second chromatography on DEAE-cellulose column Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
Gallus gallus
-
placenta
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2 key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen Gallus gallus procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
procollagen L-proline + 2-oxoglutarate + O2 key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen Homo sapiens procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?
protocollagen + 2-oxoglutarate + O2
-
Gallus gallus 4-hydroxyproline containing protocollagen + succinate + CO2
-
?
protocollagen + 2-oxoglutarate + O2
-
Homo sapiens 4-hydroxyproline containing protocollagen + succinate + CO2
-
?

Subunits

Subunits Comment Organism
More structure of the tetramer, physicochemical properties of the subunits Gallus gallus
More structure of the tetramer, physicochemical properties of the subunits Homo sapiens
tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Gallus gallus
tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Homo sapiens
tetramer alpha: 64000, beta: 62000, ratio 1 to 2 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
2-oxoglutarate
-
Gallus gallus
2-oxoglutarate
-
Homo sapiens
ascorbate requirement Gallus gallus
ascorbate requirement Homo sapiens