Literature summary for 1.14.99.29 extracted from

Quintas-Granados, L.I.; Carvajal Gamez, B.I.; Villalpando, J.L.; Ortega-Lopez, J.; Arroyo, R.; Azuara-Liceaga, E.; Alvarez-Sanchez, M.E.
Bifunctional activity of deoxyhypusine synthase/hydroxylase from Trichomonas vaginalis (2016), Biochimie, 123, 37-51 .

Search for more literature for 1.14.99.29

Inhibitors

Inhibitors	Comment	Organism	Structure
N''-guanyl-1,7-diaminoheptane	competitive inhibition	Trichomonas vaginalis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
170000	-	gel filtration	Trichomonas vaginalis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
[eIF5A]-deoxyhypusine + NADH + H+ + O2	Trichomonas vaginalis	-	[eIF5A]-hypusine + NAD+ + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Trichomonas vaginalis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[eIF5A]-deoxyhypusine + NADH + H+ + O2	-	Trichomonas vaginalis	[eIF5A]-hypusine + NAD+ + H2O	-	?

Subunits

Subunits	Comment	Organism
homotetramer	4 * 43000, recombinant enzyme, SDS-PAGE	Trichomonas vaginalis
homotetramer	4 * 41000, native enzyme, SDS-PAGE	Trichomonas vaginalis

Synonyms

Synonyms	Comment	Organism
deoxyhypusine synthase/hydroxylase	bifunctional enzyme	Trichomonas vaginalis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	dependent on	Trichomonas vaginalis

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Release 2023.1 (January 2023)