Homoserine O-succinyltransferase

In enzymology, a homoserine O-succinyltransferase (EC 2.3.1.46) is an enzyme that catalyzes the chemical reaction

succinyl-CoA + L-homoserine ${\displaystyle \rightleftharpoons }$ CoA + O-succinyl-L-homoserine

homoserine O-succinyltransferase
Homoserine O-acetyltransferase dimer, Bacillus cereus
Identifiers
EC no.	2.3.1.46
CAS no.	62213-51-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Thus, the two substrates of this enzyme are succinyl-CoA and L-homoserine, whereas its two products are CoA and O-succinyl-L-homoserine.

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-homoserine O-succinyltransferase. Other names in common use include homoserine O-transsuccinylase, and homoserine succinyltransferase. This enzyme participates in methionine metabolism and sulfur metabolism.

Structural studies

As of late 2016, three structures have been solved for this class of enzymes, with PDB accession codes 2GHR, 2H2W, and 2VDJ.