Enzyme

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     6. Ligases
        6.1 Forming carbon-oxygen bonds
            6.1.1 Ligases forming aminoacyl-tRNA and related compounds
ID:6.1.1.23
Description:Aspartate--tRNA(Asn) ligase.
Alternative Name: Nondiscriminating aspartyl-tRNA synthetase.
Cath: 3.30.1360.30; 3.30.930.10; 2.40.50.140;

3D structure

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References

External Links

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
MSA:

6.1.1.23;

Phylogenetic Tree:

6.1.1.23;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways.Becker HD, Kern D1998 Oct 279789000
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 D1998 Sep 19724658
Aminoacyl-tRNA synthesis.Ibba M, Soll D200010966471