Homoserine O-succinyltransferase
From Wikipedia, the free encyclopedia
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
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.
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[edit] Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2GHR and 2H2W.
[edit] References
- IUBMB entry for 2.3.1.46
- BRENDA references for 2.3.1.46 (Recommended.)
- PubMed references for 2.3.1.46
- PubMed Central references for 2.3.1.46
- Google Scholar references for 2.3.1.46
- 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.
[edit] External links
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- The CAS registry number for this enzyme class is 62213-51-8.