Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Evans LD,Roszak AW,Noble LJ,Robinson DA,Chalk PA,Matthews JL,Coggins JR,Price NC,Lapthorn AJdoi
10.1016/s0014-5793(02)03346-xkeywords:
subject
Has Abstractpub_date
2002-10-23 00:00:00pages
24-30issue
1-3eissn
0014-5793issn
1873-3468pii
S001457930203346Xjournal_volume
530pub_type
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