Literature summary for 1.4.3.16 extracted from

Marinoni, I.; Nonnis, S.; Monteferrante, C.; Heathcote, P.; Haertig, E.; Boettger, L.H.; Trautwein, A.X.; Negri, A.; Albertini, A.M.; Tedeschi, G.
Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis (2008), FEBS J., 275, 5090-5107.

Search for more literature for 1.4.3.16

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1	-	L-aspartate	using O2 as electron acceptor	Bacillus subtilis
1.43	-	fumarate	-	Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55000	-	monomer, gel filtration	Bacillus subtilis
115000	-	dimer, gel filtration	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P38032	-	-

Purification (Commentary)

Purification (Comment)	Organism
using NH4SO4 precipitation and using a DEAE-sepharose column	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate + fumarate	-	Bacillus subtilis	iminoaspartate + succinate	-	?
L-aspartate + O2	-	Bacillus subtilis	iminoaspartate + H2O2	-	?

Subunits

Subunits	Comment	Organism
dimer	gel filtration, 2 * 55000 Da, dimer in the absence of NaCl	Bacillus subtilis
monomer	gel filtration, monomer in the presence of 150 mM NaCl	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
L-aspartate oxidase	-	Bacillus subtilis
nadB	-	Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.18	-	L-aspartate	using O2 as electron acceptor	Bacillus subtilis
0.5	-	fumarate	-	Bacillus subtilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Bacillus subtilis

General Information

General Information	Comment	Organism
physiological function	NadB and NadA (quinolinate synthase) interact with each other. The interaction is not species-specific and both proteins are not tightly bound to one another, indicating a function as a reversible multienzyme complex	Bacillus subtilis
physiological function	NadB shows three enzymatic activities: L-aspartate-oxygen oxidoreductase activity, fumarate reductase activity, and L-aspartate-fumarate oxidoreductase activity	Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.18	-	L-aspartate	using O2 as electron acceptor	Bacillus subtilis
0.35	-	fumarate	-	Bacillus subtilis

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Release 2023.1 (January 2023)