Enzyme

Download
EC Tree
     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.4 Other carbon-nitrogen ligases
ID:6.3.4.5
Description:Argininosuccinate synthase.
Alternative Name: Citrulline--aspartate ligase.
Argininosuccinate synthetase.
Arginine succinate synthetase.
Prosite: PDOC00488;
PDB:
PDBScop
1VL2 8029044; 8029046; 8041423; 8041425; 8029044; 8029046; 8041423; 8041425; 8029044; 8029046; 8041423; 8041425; 8029044; 8029046; 8041423; 8041425;
1KP3 8025544; 8025547; 8037923; 8037926;
1KP2 8025544; 8025547; 8037923; 8037926;
1K97 8025544; 8025547; 8037923; 8037926;
1K92 8025544; 8025547; 8037923; 8037926;
 » show all

Cath: 1.10.287.40; 1.10.287.400; 1.20.5.470; 3.40.50.620; 3.90.1260.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

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.

References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.4.5
BRENDA Enzyme Link: BRENDA 6.3.4.5
KEGG Enzyme Link: KEGG6.3.4.5
BioCyc Enzyme Link: BioCyc 6.3.4.5
ExPASy Enzyme Link: ExPASy6.3.4.5
EC2PDB Enzyme Link: EC2PDB 6.3.4.5
ExplorEnz Enzyme Link: ExplorEnz 6.3.4.5
PRIAM enzyme-specific profiles Link: PRIAM 6.3.4.5
IntEnz Enzyme Link: IntEnz 6.3.4.5
MEDLINE Enzyme Link: MEDLINE 6.3.4.5
MSA:

6.3.4.5;

Phylogenetic Tree:

6.3.4.5;

Uniprot:
M-CSA:
RHEA:10932 ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](-[NH2;+0:3])=[O;H0;+0:4].[*:5]-[NH2;+0:6].[*:7]-[O;H0;+0:8]-[P;H0;+0:9](-[*:10])(=[*:11])-[*:12]>>[*:1]-[C;H0;+0:2](=[NH;+0:3])-[NH;+0:6]-[*:5].[*:7]-[OH;+0:8].[*:10]-[P;H0;+0:9](=[*:11])(-[*:12])-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells.Shaheen N, Kobayashi K, Terazono H, Fukushige T, Horiuchi M, Saheki T1994-19958792870
Measurement of positional isotope exchange rates in enzyme-catalyzed reactions by fast atom bombardment mass spectrometry: application to argininosuccinate synthetase.Hilscher LW, Hanson CD, Russell DH, Raushel FM1985 Oct 82867775
Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation.Diez-Fernandez C, Wellauer O, Gemperle C, Rüfenacht V, Fingerhut R, Häberle J2016 Oct27287393
Structure of human argininosuccinate synthetase.Karlberg T, Collins R, van den Berg S, Flores A, Hammarström M, Högbom M, Holmberg Schiavone L, Uppenberg J2008 Mar18323623
Almost all about citrulline in mammals.Curis E, Nicolis I, Moinard C, Osowska S, Zerrouk N, Bénazeth S, Cynober L2005 Nov16082501
Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction.Goto M, Omi R, Miyahara I, Sugahara M, Hirotsu K2003 Jun 2012684518
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis.Lemke CT, Howell PL2001 Dec11738042