EC Tree |
6. Ligases |
6.1 Forming carbon-oxygen bonds |
6.1.1 Ligases forming aminoacyl-tRNA and related compounds |
ID: | 6.1.1.12 | ||
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Description: | Aspartate--tRNA ligase. | ||
Alternative Name: |
Aspartyl-tRNA synthetase. Aspartic acid translase. | ||
Prosite: | PDOC00363; | ||
PDB: |
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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 6.1.1.12 |
BRENDA Enzyme Link: | BRENDA 6.1.1.12 |
KEGG Enzyme Link: | KEGG6.1.1.12 |
BioCyc Enzyme Link: | BioCyc 6.1.1.12 |
ExPASy Enzyme Link: | ExPASy6.1.1.12 |
EC2PDB Enzyme Link: | EC2PDB 6.1.1.12 |
ExplorEnz Enzyme Link: | ExplorEnz 6.1.1.12 |
PRIAM enzyme-specific profiles Link: | PRIAM 6.1.1.12 |
IntEnz Enzyme Link: | IntEnz 6.1.1.12 |
MEDLINE Enzyme Link: | MEDLINE 6.1.1.12 |
RHEA:19649 | ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp) |
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 |
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Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes. | Becker HD, Reinbolt J, Kreutzer R, Giegé R, Kern D | 1997 Jul 22 | 9220965 |
Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. | Neuenfeldt A, Lorber B, Ennifar E, Gaudry A, Sauter C, Sissler M, Florentz C | 2013 Feb 1 | 23275545 |
Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. | Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M | 2005 Mar 29 | 15779907 |
Expanding tRNA recognition of a tRNA synthetase by a single amino acid change. | Feng L, Tumbula-Hansen D, Toogood H, Soll D | 2003 May 13 | 12730374 |
Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain. | Charron C, Roy H, Blaise M, Giegé R, Kern D | 2003 Apr 1 | 12660169 |
Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase. | Becker HD, Roy H, Moulinier L, Mazauric MH, Keith G, Kern D | 2000 Mar 28 | 10727213 |