Mirza_2005_Biochemistry_44_15768

Reference

Title : Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha\/beta-hydrolases - Mirza_2005_Biochemistry_44_15768
Author(s) : Mirza IA , Nazi I , Korczynska M , Wright GD , Berghuis AM
Ref : Biochemistry , 44 :15768 , 2005
Abstract :

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.

PubMedSearch : Mirza_2005_Biochemistry_44_15768
PubMedID: 16313180
Gene_locus related to this paper: haein-metx

Related information

Gene_locus haein-metx
Family haein-metx    Homoserine_transacetylase
Structure haein-metx    Homoserine_transacetylase    2B61

Citations formats

Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM (2005)
Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha\/beta-hydrolases
Biochemistry 44 :15768

Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM (2005)
Biochemistry 44 :15768