Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mirza IA,Nazi I,Korczynska M,Wright GD,Berghuis AM

doi

10.1021/bi051951y

subject

Has Abstract

pub_date

2005-12-06 00:00:00

pages

15768-73

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

44

pub_type

杂志文章