Enzyme

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     6. Ligases
        6.1 Forming carbon-oxygen bonds
            6.1.1 Ligases forming aminoacyl-tRNA and related compounds
ID:6.1.1.12
Description:Aspartate--tRNA ligase.
Alternative Name: Aspartyl-tRNA synthetase.
Aspartic acid translase.
Prosite: PDOC00363;
PDB:
PDBScop
Cath: 3.30.1360.30; 3.30.930.10; 2.40.50.140;

3D structure

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References

External Links

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
MSA:

6.1.1.12;

Phylogenetic Tree:

6.1.1.12;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
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 D1997 Jul 229220965
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 C2013 Feb 123275545
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 M2005 Mar 2915779907
Expanding tRNA recognition of a tRNA synthetase by a single amino acid change.Feng L, Tumbula-Hansen D, Toogood H, Soll D2003 May 1312730374
Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain.Charron C, Roy H, Blaise M, Giegé R, Kern D2003 Apr 112660169
Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase.Becker HD, Roy H, Moulinier L, Mazauric MH, Keith G, Kern D2000 Mar 2810727213