1h05: Difference between revisions
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==Overview== | ==Overview== | ||
The interactions between the polyanionic ligands phosphate and sulphate | 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 Structure== | ==About this Structure== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Coggins, J | [[Category: Coggins, J R.]] | ||
[[Category: Lapthorn, A | [[Category: Lapthorn, A J.]] | ||
[[Category: Roszak, A | [[Category: Roszak, A W.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
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[[Category: shikimate pathway]] | [[Category: shikimate pathway]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:56 2008'' | ||
Revision as of 13:55, 21 February 2008
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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 as ligand. Active as 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Known structural/functional Site: . 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
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