NAD+ synthase

{{Short description|Enzyme}}

{{infobox enzyme

| Name = NAD+ synthetase

| EC_number = 6.3.1.5

| CAS_number = 9032-69-3

| GO_code = 0008795

| image =

| width =

| caption =

}}

In enzymology, a NAD+ synthetase ({{EnzExplorer|6.3.1.5}}) is an enzyme that catalyzes the chemical reaction

:ATP + deamido-NAD+ + NH3 \rightleftharpoons AMP + diphosphate + NAD+

The 3 substrates of this enzyme are ATP, deamido-NAD+, and NH3, whereas its 3 products are AMP, diphosphate, and NAD+.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthetase). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names in common use include NAD+ synthetase, NAD+ synthetase, nicotinamide adenine dinucleotide synthetase, and diphosphopyridine nucleotide synthetase. This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism.

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1WXE}}, {{PDB link|1WXF}}, {{PDB link|1WXG}}, {{PDB link|1WXH}}, {{PDB link|1WXI}}, {{PDB link|1XNG}}, {{PDB link|1XNH}}, {{PDB link|2E18}}, {{PDB link|2PZ8}}, {{PDB link|2PZA}}, and {{PDB link|2PZB}}.

References

{{reflist|1}}

  • {{cite journal | vauthors = Spencer RL, Preiss J | date = 1967 | title = Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphospyridine nucleotide synthetase from Escherichia coli b | journal = J. Biol. Chem. | volume = 242 | pages = 385–92 | pmid = 4290215 | issue = 3 | doi = 10.1016/S0021-9258(18)96282-4 | doi-access = free }}

{{Ligases CO CS and CN}}

{{Enzymes}}

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Category:EC 6.3.1

Category:NADH-dependent enzymes

Category:Enzymes of known structure

{{6.3-enzyme-stub}}