| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor |
| ID: | 6.3.5.4 | ||
|---|---|---|---|
| Description: | Asparagine synthase (glutamine-hydrolyzing). | ||
| Alternative Name: |
Glutamine-dependent asparagine synthetase. Asparagine synthetase B. Asparagine synthetase (glutamine-hydrolyzing). AS-B. | ||
| Prosite: | PDOC00406; | ||
| PDB: |
|
||
| Cath: | 3.40.50.620; 3.60.20.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 6.3.5.4 |
| BRENDA Enzyme Link: | BRENDA 6.3.5.4 |
| KEGG Enzyme Link: | KEGG6.3.5.4 |
| BioCyc Enzyme Link: | BioCyc 6.3.5.4 |
| ExPASy Enzyme Link: | ExPASy6.3.5.4 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.5.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.5.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.5.4 |
| IntEnz Enzyme Link: | IntEnz 6.3.5.4 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.5.4 |
| RHEA:12228 | ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[*:5]-[O;H0;+0:6]-[P;H0;+0:7](-[*:8])(=[*:9])-[*:10].[*:11]=[C;H0;+0:12](-[*:13])-[OH;+0:14].[OH2;+0:15]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:14].[*:5]-[OH;+0:6].[*:8]-[P;H0;+0:7](=[*:9])(-[*:10])-[OH;+0:15].[*:11]=[C;H0;+0:12](-[*:13])-[NH2;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mechanistic issues in asparagine synthetase catalysis. | Richards NG, Schuster SM | 1998 | 9559053 |
| Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. | Boehlein SK, Richards NG, Schuster SM | 1994 Mar 11 | 7907328 |
| Asparagine biosynthesis by the Novikoff Hepatoma isolation, purification, property, and mechanism studies of the enzyme system. | Patterson MK Jr, Orr GR | 1968 Jan 25 | 4295091 |
| Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli. | Tesson AR, Soper TS, Ciustea M, Richards NG | 2003 May 1 | 12706338 |
| Channeling of substrates and intermediates in enzyme-catalyzed reactions. | Huang X, Holden HM, Raushel FM | 2001 | 11395405 |
| Three-dimensional structure of escherichia coli asparagine synthetase B: A short journey from substrate to product | Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I I | 2000 Jun 20 | 10852734 |
| Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. | Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I | 1999 Dec 7 | 10587437 |