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Literature summary extracted from

  • Annunen, P.; Koivunen, P.; Kivirikko, K.I.
    Cloning of the a subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties (1999), J. Biol. Chem., 274, 6790-6796.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.2 cloning of the alpha subunit of the enzyme, coexpression in insect cells with the Drosophila protein-disulfide isomerase polypeptide produces an active enzyme tetramer, coexpression in insect cells with human protein-disulfide isomerase polypeptide produces also small amounts of a hybrid tetramer Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.2 R490H the mutation reduces the percentage of uncoupled decarboxylation Drosophila melanogaster
1.14.11.2 R490S the mutation increases the Km for 2-oxoglutarate, reduces the reaction velocity and increases the percentage of uncoupled decarboxylation Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.2 poly(L-proline) MW: 7000 and 44000 Drosophila melanogaster
1.14.11.2 poly(L-proline) MW: 7000 and 44000 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.2 0.021
-
 (Pro-Pro-Gly)10 type I enzyme Homo sapiens
1.14.11.2 0.022
-
 2-oxoglutarate type I and type II enzymes Homo sapiens
1.14.11.2 0.084
-
 2-oxoglutarate wild-type enzyme Drosophila melanogaster
1.14.11.2 0.088
-
 (Pro-Pro-Gly)10 type I enzyme Homo sapiens
1.14.11.2 0.106
-
 2-oxoglutarate R490H mutant Drosophila melanogaster
1.14.11.2 0.106
-
 2-oxoglutarate R490S mutant Drosophila melanogaster
1.14.11.2 0.26
-
 (L-Pro-L-Pro-Gly)10
-
 Drosophila melanogaster

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.2 Fe2+ Km: 0.003 mM Drosophila melanogaster
1.14.11.2 Fe2+ type I enzyme: Km 0.003 mM, type II enzyme: Km 0.004 mM Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.2 Drosophila melanogaster
-
-
-
1.14.11.2 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.2 larva
-
 Drosophila melanogaster
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.11.2 additional information
-
-
 Homo sapiens
1.14.11.2 additional information
-
 enzyme activity of mutants Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.2 (L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
-
 Drosophila melanogaster (L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
 r
1.14.11.2 (Pro-Pro-Gly)10 + 2-oxoglutarate + O2
-
 Homo sapiens ? + succinate + CO2
-
 ?
1.14.11.2 (Pro-Pro-Gly)n + 2-oxoglutarate + O2 n: 1,5,10 Drosophila melanogaster (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 n: 1,5,10 ?
1.14.11.2 (Pro-Pro-Gly)n + 2-oxoglutarate + O2 n: 1,5,10 Homo sapiens (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 n: 1,5,10 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.2 More
-
 Homo sapiens
1.14.11.2 More amino acid sequence of the alpha subunit and its comparison with those of the human alpha-I and alpha-II subunits and the Caenorhabditis elegans alpha subunit Drosophila melanogaster
1.14.11.2 tetramer
-
 Homo sapiens
1.14.11.2 tetramer the alpha subunit forms enzyme alpha2 beta2 tetramers with the Drosophila and human protein-disulfide isomerase polypeptides, nondenaturing-PAGE and Coomassie Blue-staining Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.11.2 ascorbate Km: 0.3 mM Drosophila melanogaster
1.14.11.2 ascorbate type I enzyme: Km 0.32 mM, type II enzyme: Km 0.34 mM Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.11.2 0.00002
-
 poly(L-proline) MW: 44000, human type I enzyme Homo sapiens
1.14.11.2 0.0006
-
 poly(L-proline) MW: 7000, human type I enzyme Homo sapiens
1.14.11.2 0.0029
-
 poly(L-proline) MW: 44000 Drosophila melanogaster
1.14.11.2 0.018
-
 poly(L-proline) MW: 7000 Drosophila melanogaster
1.14.11.2 0.022
-
 poly(L-proline) MW: 44000, human type II enzyme Homo sapiens
1.14.11.2 0.095
-
 poly(L-proline) MW: 7000, type II enzyme Homo sapiens