Homoserine O-succinyltransferase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
homoserine O-succinyltransferase
Identifiers
EC number 2.3.1.46
CAS number 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 / EGO

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

succinyl-CoA + L-homoserine \rightleftharpoons CoA + O-succinyl-L-homoserine

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[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2GHR and 2H2W.

References[edit]

  • Rowbury RJ and Woods DD (1964). "O-Succinylhomoserine as an intermediate in the synthesis of cystathionine by Escherichia coli". J. Gen. Microbiol. 36: 341–358. doi:10.1099/00221287-36-3-341. PMID 14217349.