Literature summary for 2.7.1.23 extracted from

Poncet-Montange, G.; Assairi, L.; Arold, S.; Pochet, S.; Labesse, G.
NAD kinases use substrate-assisted catalysis for specific recognition of NAD (2007), J. Biol. Chem., 282, 33925-33934.

Search for more literature for 2.7.1.23

Application

Application	Comment	Organism
additional information	conserved GGDGT motif of NADKs	Listeria monocytogenes

Cloned(Commentary)

Cloned (Comment)	Organism
into vector pET22b and expressed in Escherichia coli BL21(DE3)/pDIA17	Listeria monocytogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
by hanging-drop-based sparse-matrix screening strategy. NAD kinase crystallized in complex with its substrate NAD, its product NADP, or two synthesized NAD mimics, at near 2 A resolution. D45N mutant using the I222 5'-thioacetyladenosine-bound crystal form, to 2.2 A resolution, and mutant H223E	Listeria monocytogenes

Protein Variants

Protein Variants	Comment	Organism
D45N	only minor changes, its active site is similar to that of the wild-type enzyme with the ligand present in the same conformation. The asparagine adopts the same buried conformation as the aspartate but does not form any hydrogen bond with NAD. Mutation results in a 10fold decrease in activity	Listeria monocytogenes
H223E	is twice less active than the wild-type on the biologically relevant substrate NAD. In contrast, its activity toward di-(5'-thioadenosine) is increased 2fold	Listeria monocytogenes

Inhibitors

Inhibitors	Comment	Organism	Structure
5'-thioacetyladenosine	-	Listeria monocytogenes
di-(5'-thioadenosine)	-	Listeria monocytogenes
NADP	-	Listeria monocytogenes

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1	-	NAD+	wild-type	Listeria monocytogenes
2.1	-	ATP	mutant D45N	Listeria monocytogenes
2.8	-	ATP	wild-type	Listeria monocytogenes

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Listeria monocytogenes

Organism

Organism	UniProt	Comment	Textmining
Listeria monocytogenes	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
affinity chromatography and gel filtration	Listeria monocytogenes

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + NAD+	Asp-45 is a key residue for the catalytic activity of NADK1	Listeria monocytogenes	ADP + NADP+	-	?
di-adenosine diphosphate	-	Listeria monocytogenes	?	-	?

Subunits

Subunits	Comment	Organism
homotetramer	crystallography	Listeria monocytogenes

Synonyms

Synonyms	Comment	Organism
EC 2.7.1.23	related	Listeria monocytogenes
NAD kinase 1	-	Listeria monocytogenes
NADK1	-	Listeria monocytogenes

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.41	-	NAD+	mutant D45N, in the presence of 0.5 mM ATP	Listeria monocytogenes
1.34	-	NAD+	mutant D45N, in the presence of 4 mM ATP	Listeria monocytogenes
2.03	-	ATP	mutant D45N	Listeria monocytogenes
3.62	-	NAD+	wild-type, in the presence of 0.5 mM ATP	Listeria monocytogenes
13.12	-	NAD+	wild-type, in the presence of 4 mM ATP	Listeria monocytogenes
13.78	-	ATP	wild-type	Listeria monocytogenes

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.02	-	di-(5'-thioadenosine)	-	Listeria monocytogenes
0.04	-	NADP	-	Listeria monocytogenes
3.6	-	5'-thioacetyladenosine	-	Listeria monocytogenes

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Release 2023.1 (January 2023)