1hl2
CRYSTAL STRUCTURE OF N-ACETYLNEURAMINATE LYASE FROM E. COLI MUTANT L142R IN COMPLEX WITH B-HYDROXYPYRUVATE
|
OverviewOverview
N-acetylneuraminate lyase (NAL) and dihydrodipicolinate synthase (DHDPS), belong to the NAL subfamily of (betaalpha)(8)-barrels. They share a common, catalytic step but catalyze reactions in different biological pathways. By, rational design, we have introduced various mutations into the NAL, scaffold from Escherichia coli to switch the activity toward DHDPS. These, mutants were tested with respect to their catalytic properties in vivo and, in vitro as well as their stability. One point mutation (L142R) was, sufficient to create an enzyme that could complement a bacterial auxotroph, lacking the gene for DHDPS as efficiently as DHDPS itself. In vitro, this, mutant had an increased DHDPS activity of up to 19-fold as defined by the, specificity constant k(cat)K(M) for the new substrate, ... [(full description)]
About this StructureAbout this Structure
1HL2 is a [Single protein] structure of sequence from [Escherichia coli] with 3PY as [ligand]. Active as [[1]], with EC number [4.1.3.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity., Joerger AC, Mayer S, Fersht AR, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5694-9. Epub 2003 Apr 23. PMID:12711733
Page seeded by OCA on Mon Oct 29 22:05:31 2007