Enzyme

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     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.4 Other carbon-nitrogen ligases
ID:6.3.4.4
Description:Adenylosuccinate synthase.
Alternative Name: Succinoadenylic kinosynthetase.
IMP--aspartate ligase.
Adenylosuccinate synthetase.
Prosite: PDOC00444;
PDB:
PDBScop
5K7X 8089708; 8089709; 8089708; 8089709; 8089708; 8089709; 8089708; 8089709; 8089708; 8089709; 8089708; 8089709;
2D7U 8089708; 8089709;
1LNY 8089706; 8089707; 8089706; 8089707;
1IWE 8089706; 8089707; 8089706; 8089707;
2DGN 8089706; 8089707;
 » show all

Cath: 1.10.300.10; 3.90.170.10; 3.40.440.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.4.4
BRENDA Enzyme Link: BRENDA 6.3.4.4
KEGG Enzyme Link: KEGG6.3.4.4
BioCyc Enzyme Link: BioCyc 6.3.4.4
ExPASy Enzyme Link: ExPASy6.3.4.4
EC2PDB Enzyme Link: EC2PDB 6.3.4.4
ExplorEnz Enzyme Link: ExplorEnz 6.3.4.4
PRIAM enzyme-specific profiles Link: PRIAM 6.3.4.4
IntEnz Enzyme Link: IntEnz 6.3.4.4
MEDLINE Enzyme Link: MEDLINE 6.3.4.4
MSA:

6.3.4.4;

Phylogenetic Tree:

6.3.4.4;

Uniprot:
M-CSA:
RHEA:15753 GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[O;H0;+0:4]-[P;H0;+0:5](=[*:6])(-[*:7])-[*:8].[*:9]:[nH;+0:10]:[c;H0;+0:11](:[*:12])=[O;H0;+0:13]>>[*:3]-[OH;+0:4].[*:9]:[n;H0;+0:10]:[c;H0;+0:11](:[*:12])-[NH;+0:2]-[*:1].[*:6]=[P;H0;+0:5](-[*:7])(-[*:8])-[OH;+0:13]
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References

TitleAuthorsDatePubMed ID
Relationship of conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase.Wang W, Hou Z, Honzatko RB, Fromm HJ1997 Jul 49202000
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli.Poland BW, Bruns C, Fromm HJ, Honzatko RB1997 Jun 139182542
Residues essential for catalysis and stability of the active site of Escherichia coli adenylosuccinate synthetase as revealed by directed mutation and kinetics.Kang C, Sun N, Poland BW, Gorrell A, Honzatko RB, Fromm HJ1997 May 29115248
Studies of ligand binding to Escherichia coli adenylosuccinate synthetase.Soans C, Fromm HJ1991 Nov 151929424
Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli.Choe JY, Poland BW, Fromm HJ, Honzatko RB1999 May 2510346917