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 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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

References

    • Rowbury RJ, Woods DD (September 1964). "O-Succinylhomoserine as an Intermediate in the Synthesis of Cystathionine by Escherichia coli". Journal of General Microbiology. 36 (3): 341–58. doi:10.1099/00221287-36-3-341. PMID 14217349.


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