EC number:6.3.1.5
Enzyme
Download| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases) |
| ID: | 6.3.1.5 |
|---|---|
| Description: | NAD(+) synthase. |
| Alternative Name: |
NAD(+) synthetase. |
| Cath: | 1.10.10.1140; 3.40.50.620; 3.60.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 6.3.1.5 |
| BRENDA Enzyme Link: | BRENDA 6.3.1.5 |
| KEGG Enzyme Link: | KEGG6.3.1.5 |
| BioCyc Enzyme Link: | BioCyc 6.3.1.5 |
| ExPASy Enzyme Link: | ExPASy6.3.1.5 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.1.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.1.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.1.5 |
| IntEnz Enzyme Link: | IntEnz 6.3.1.5 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.1.5 |
| RHEA:21188 | ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+) |
| RULE(radius=1) | [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]=[C;H0;+0:8](-[*:9])-[OH;+0:10].[NH3;+0:11]>>[*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:10].[*:7]=[C;H0;+0:8](-[*:9])-[NH2;+0:11] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase. | Willison JC, Tissot G | 1994 Jun | 8195100 |
| The outB gene of Bacillus subtilis codes for NAD synthetase. | Nessi C, Albertini AM, Speranza ML, Galizzi A | 1995 Mar 17 | 7890752 |
| Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphospyridine nucleotide synthetase from Escherichia coli b. | Spencer RL, Preiss J | 1967 Feb 10 | 4290215 |
| Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis. | McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, DeLucas LJ, Brouillette WJ, Brouillette CG | 2007 Aug | 17642516 |