Literature summary for 1.17.1.5 extracted from

Gladyshev, V.N.; Khangulov, S.V.; Stadtman, T.C.
Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme (1994), Proc. Natl. Acad. Sci. USA, 91, 232-236.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
23000	-	1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE	Eubacterium barkeri
33000	-	1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE	Eubacterium barkeri
37000	-	1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE	Eubacterium barkeri
50000	-	1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE	Eubacterium barkeri
160000	-	native PAGE	Eubacterium barkeri

Organism

Organism	UniProt	Comment	Textmining
Eubacterium barkeri	-	-	-

Oxidation Stability

Oxidation Stability	Organism
oxygen-sensitive enzyme	Eubacterium barkeri

Purification (Commentary)

Purification (Comment)	Organism
-	Eubacterium barkeri

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	more values for specific activities in crude extract	Eubacterium barkeri
4.4	-	purified enzyme, Difco yeast extract without selenium as growth medium	Eubacterium barkeri
20	-	purified enzyme, average value, Difco yeast extract with selenium as growth medium	Eubacterium barkeri

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nicotinate + H2O + NADP+	NADP+ or various dyes as electron acceptors	Eubacterium barkeri	6-hydroxynicotinate + NADPH	with NADPH as substrate, enzyme exhibits NADPH oxidase activity in presence of oxygen	r

Subunits

Subunits	Comment	Organism
heterotetramer	1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE	Eubacterium barkeri

Cofactor

Cofactor	Comment	Organism	Structure
4Fe-4S-center	enzyme contains iron-sulfur clusters, [2Fe-2S] centers	Eubacterium barkeri
FAD	-	Eubacterium barkeri
molybdenum cofactor	-	Eubacterium barkeri
molybdopterin	molybdenum in the molybdopterin cofactor is coordinated directly with a dissociable selenium moiety, molybdenum center plays a role in the reaction step involving hydroxylation of the heterocyclic ring with oxygen derived from water	Eubacterium barkeri
additional information	enzyme contains a dissociable selenium moiety, which is coordinated directly with molybdenum in the molybdopterin cofactor, selenium is essential for enzyme activity, molar ratio of selenium to enzyme is 0.4-0.8, enzyme contains 1 g selenium per mol of native active enzyme, selenium is completely dissociated from protein in the SDS-gel	Eubacterium barkeri
NADP+	NADP+ as ultimate electron acceptor, can be replaced by various dyes	Eubacterium barkeri
NADPH	NADPH oxidase activity in the presence of oxygen	Eubacterium barkeri

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Release 2023.1 (January 2023)