Literature summary for 1.14.11.2 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.

Search for more literature for 1.14.11.2

Cloned(Commentary)

Cloned (Comment)	Organism
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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
larva	-	Drosophila melanogaster	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(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
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2	-	Homo sapiens	? + succinate + CO2	-	?
(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	?
(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

Subunits	Comment	Organism
More	-	Homo sapiens
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
tetramer	-	Homo sapiens
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

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

Ki Value [mM]

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

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Release 2023.1 (January 2023)