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Arginine N-succinyltransferase

From Wikipedia, the free encyclopedia
arginine N-succinyltransferase
Identifiers
EC no.2.3.1.109
CAS no.99676-48-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction

succinyl-CoA + L-arginine CoA + N2-succinyl-L-arginine

Thus, the two substrates of this enzyme are succinyl-CoA and L-arginine, whereas its two products are CoA and N2-succinyl-L-arginine.[1]

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:L-arginine N2-succinyltransferase. Other names in common use include arginine succinyltransferase, AstA, arginine and ornithine N2-succinyltransferase, AOST, AST, and succinyl-CoA:L-arginine 2-N-succinyltransferase. This enzyme participates in arginine and proline metabolism.

Structural studies

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As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YLE.

References

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  1. ^ "N(2)-Succinyl-L-arginine (Compound) on National Center for Biotechnology Information USA".

Further reading

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