EC Tree |
6. Ligases |
6.1 Forming carbon-oxygen bonds |
6.1.1 Ligases forming aminoacyl-tRNA and related compounds |
ID: | 6.1.1.23 |
---|---|
Description: | Aspartate--tRNA(Asn) ligase. |
Alternative Name: |
Nondiscriminating aspartyl-tRNA synthetase. |
Cath: | 3.30.1360.30; 3.30.930.10; 2.40.50.140; |
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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 6.1.1.23 |
BRENDA Enzyme Link: | BRENDA 6.1.1.23 |
KEGG Enzyme Link: | KEGG6.1.1.23 |
BioCyc Enzyme Link: | BioCyc 6.1.1.23 |
ExPASy Enzyme Link: | ExPASy6.1.1.23 |
EC2PDB Enzyme Link: | EC2PDB 6.1.1.23 |
ExplorEnz Enzyme Link: | ExplorEnz 6.1.1.23 |
PRIAM enzyme-specific profiles Link: | PRIAM 6.1.1.23 |
IntEnz Enzyme Link: | IntEnz 6.1.1.23 |
MEDLINE Enzyme Link: | MEDLINE 6.1.1.23 |
RHEA:18349 | ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx) |
RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[O;H0;+0:6]-[P;H0;+0:7](-[*:8])(=[*:9])-[*:10].[*:11]-[OH;+0:12]>>[*:11]-[O;H0;+0:12]-[C;H0;+0:2](-[*:1])=[*:3].[*:5]-[OH;+0:6].[*:8]-[P;H0;+0:7](=[*:9])(-[*:10])-[OH;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. | Becker HD, Kern D | 1998 Oct 27 | 9789000 |
Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation. | Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D | 1998 Sep 1 | 9724658 |
Aminoacyl-tRNA synthesis. | Ibba M, Soll D | 2000 | 10966471 |