Literature summary for 1.14.11.29 extracted from

Osipyants, A.I.; Poloznikov, A.A.; Smirnova, N.A.; Hushpulian, D.M.; Khristichenko, A.Y.; Chubar, T.A.; Zakhariants, A.A.; Ahuja, M.; Gaisina, I.N.; Thomas, B.; Brown, A.M.; Gazaryan, I.G.; Tishkov, V.I.
L-ascorbic acid A true substrate for HIF prolyl hydroxylase? (2018), Biochimie, 147, 46-54 .

Search for more literature for 1.14.11.29

Crystallization (Commentary)

Crystallization (Comment)	Organism
L-ascorbic acid can be docked in the binding site of 2-oxoglutarate and may chelate the iron ion, D-ascorbate cannot be docked	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
adaptaquin	-	Homo sapiens
ciclopirox	iron chelator	Homo sapiens
dimethyloxalyl glycine	mimicks 2-oxoglutarate binding mode	Homo sapiens
ethyl 3,4-dihydroxybenzoate	iron chelator that can fit inside the active center	Homo sapiens
FG-4592	mimicks 2-oxoglutarate binding mode	Homo sapiens
IOX2	mimicks 2-oxoglutarate binding mode	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9GZT9	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
SH-SY5Y cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-ascorbate + 2-oxoglutarate + O2	L-ascorbate is a co-substrate of HIF prolyl hydroxylase PHD that may compete for the binding site of 2-oxoglutarate in the enzyme active center	Homo sapiens	? + succinate + CO2	-	?

Synonyms

Synonyms	Comment	Organism
Egl nine homolog 1	-	Homo sapiens
EGLN1	-	Homo sapiens
PHD2	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)