Homoserine O-succinyltransferase

Homoserine O-succinyltransferase

In enzymology, a homoserine O-succinyltransferase 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

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

References

  • Rowbury RJ and Woods DD "O-Succinylhomoserine as an intermediate in the synthesis of cystathionine by Escherichia coli". J. Gen. Microbiol. 36 341–358.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes

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