Structural highlights
Function
[METX_HAEIN] Involved in the methionine biosynthesis. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-homoserine to yield O-acetyl-L-homoserine.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase structural superfamily. The active site of the enzyme is located near the end of a deep tunnel formed by the juxtaposition of two domains and incorporates a catalytic triad involving Ser143, His337, and Asp304. A structural basis is given for the observed double displacement kinetic mechanism of homoserine transacetylase. Furthermore, the properties of the tunnel provide a rationale for how homoserine transacetylase catalyzes a transferase reaction vs hydrolysis, despite extensive similarity in active site architecture to hydrolytic enzymes.
Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases.,Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM Biochemistry. 2005 Dec 6;44(48):15768-73. PMID:16313180[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Born TL, Franklin M, Blanchard JS. Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase. Biochemistry. 2000 Jul 25;39(29):8556-64. PMID:10913262
- ↑ Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM. Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases. Biochemistry. 2005 Dec 6;44(48):15768-73. PMID:16313180 doi:http://dx.doi.org/10.1021/bi051951y
