IntEnz - EC 6.3.4.5

EC 6 - Ligases

EC 6.3 - Forming carbon-nitrogen bonds

EC 6.3.4 - Other carbon—nitrogen ligases

EC 6.3.4.5 - Argininosuccinate synthase

IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 6.3.4.5

Names

Accepted name:

argininosuccinate synthase

Other names:

arginine succinate synthetase
argininosuccinate synthetase
argininosuccinic acid synthetase
arginosuccinate synthetase
citrulline—aspartate ligase

Systematic name:

L-citrulline:L-aspartate ligase (AMP-forming)

Reaction

10932 [IUBMB]

ATP

ATP

Name origin: UniProt - CHECKED (C)

CHEBI:30616

Formula: C10H12N5O13P3
Charge: -4

ChEBI compound status: CHECKED (C)

+

L-aspartate

L-aspartate

Name origin: UniProt - CHECKED (C)

CHEBI:29991

Formula: C4H6NO4
Charge: -1

ChEBI compound status: CHECKED (C)

+

L-citrulline

L-citrulline

Name origin: UniProt - CHECKED (C)

CHEBI:57743

Formula: C6H13N3O3
Charge: 0

ChEBI compound status: CHECKED (C)

=

2-(N^ω-L-arginino)succinate

2-(N(omega)-L-arginino)succinate

Name origin: UniProt - CHECKED (C)

CHEBI:57472

Formula: C10H17N4O6
Charge: -1

ChEBI compound status: CHECKED (C)

+

AMP

AMP

Name origin: UniProt - CHECKED (C)

CHEBI:456215

Formula: C10H12N5O7P
Charge: -2

ChEBI compound status: CHECKED (C)

+

diphosphate

diphosphate

Name origin: UniProt - CHECKED (C)

CHEBI:33019

Formula: HO7P2
Charge: -3

ChEBI compound status: CHECKED (C)

+

H⁺

H(+)

Name origin: UniProt - CHECKED (C)

CHEBI:15378

Formula: H
Charge: 1

ChEBI compound status: CHECKED (C)

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway

Protein domains and families: PROSITE:PDOC00488

Structural data: CSA , EC2PDB

Gene Ontology: GO:0004055

CAS Registry Number: 9023-58-9

UniProtKB/Swiss-Prot: (607) [show] [UniProt]

References

Ratner, S.

Urea synthesis and metabolism of arginine and citrulline.

Adv. Enzymol. Relat. Subj. Biochem. 15: 319-387 (1954).
Schuegraf, A., Ratner, S. and Warner, R.C.

Free energy changes of the argininosuccinate synthetase reaction and of the hydrolysis of the inner pyrophosphate bond of adenosine triphosphate.

J. Biol. Chem. 235: 3597-3602 (1960). [PMID: 13748745]

[EC 6.3.4.5 created 1961]