Literature summary for 1.14.11.2 extracted from

Veijola, J.; Koivunen, P.; Annunen, P.; Pihlajaniemi, T.; Kivirikko, K.I.
Cloning, baculovirus expression, and characterization of the a subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This a subunit forms an active ab dimer with the human protein disulfide isomerase/b subunit (1994), J. Biol. Chem., 269, 26746-26753.

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Cloned(Commentary)

Cloned (Comment)	Organism
cloning of the alpha subunit of the enzyme, expression of the alpha subunit together with human protein disulfide isomerase/beta subunit in insect cells by baculovirus vectors	Caenorhabditis elegans

Inhibitors

Inhibitors	Comment	Organism	Structure
poly(L-proline)	not inhibitory	Caenorhabditis elegans
Pyridine 2,4-dicarboxylate	recombinant enzyme, competitive inhibitor with respect to Fe2+ and 2-oxoglutarate	Caenorhabditis elegans
Zn2+	recombinant enzyme, competitive inhibition with respect to Fe2+ and 2-oxoglutarate	Caenorhabditis elegans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.015	-	(L-Pro-L-Pro-Gly)10	recombinant enzyme	Caenorhabditis elegans
0.02	-	2-oxoglutarate	recombinant enzyme	Caenorhabditis elegans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	recombinant enzyme: Km 0.005 mM	Caenorhabditis elegans

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120000	-	recombinant enzyme, gel filtration	Caenorhabditis elegans

Organism

Organism	UniProt	Comment	Textmining
Caenorhabditis elegans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
of the recombinant enzyme, using anion exchange chromatography on a DEAE-cellulose column and two gel filtration steps	Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2	-	Caenorhabditis elegans	(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2	-	r
(Pro-Pro-Gly)n + 2-oxoglutarate + O2	n: 1,5,10	Caenorhabditis elegans	(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2	n: 1,5,10	?
poly(L-Pro) + 2-oxoglutarate + O2	do not serve as substrate, assayed with recombinant enzyme	Caenorhabditis elegans	poly(4-hydroxyproline) + succinate + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	recombinant enzyme, alpha beta, ratio: 1 to 1	Caenorhabditis elegans

Cofactor

Cofactor	Comment	Organism	Structure
ascorbate	recombinant enzyme, Km: 0.3 mM	Caenorhabditis elegans

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Release 2023.1 (January 2023)