1h05: Difference between revisions
No edit summary |
No edit summary |
||
| Line 25: | Line 25: | ||
[[Category: shikimate pathway]] | [[Category: shikimate pathway]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:24:22 2007'' | ||
Revision as of 16:19, 30 October 2007
|
3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE
OverviewOverview
The interactions between the polyanionic ligands phosphate and sulphate, and the type II dehydroquinases from Streptomyces coelicolor and, Mycobacterium tuberculosis have been characterised using a combination of, structural and kinetic methods. From both approaches, it is clear that, interactions are more complex in the case of the latter enzyme. The data, provide new insights into the differences between the two enzymes in terms, of substrate recognition and catalytic efficiency and may also explain the, relative potencies of rationally designed inhibitors. An improved route to, the synthesis of the substrate 3-dehydroquinic acid (dehydroquinate) is, described.
About this StructureAbout this Structure
1H05 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with SO4 as [ligand]. Active as [3-dehydroquinate dehydratase], with EC number [4.2.1.10]. Structure known Active Site: SO1. Full crystallographic information is available from [OCA].
ReferenceReference
Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions., Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ, FEBS Lett. 2002 Oct 23;530(1-3):24-30. PMID:12387860
Page seeded by OCA on Tue Oct 30 15:24:22 2007