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Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions 1
Author(s) -
Evans Lewis D.B,
Roszak Aleksander W,
Noble Lorna J,
Robinson David A,
Chalk Peter A,
Matthews Jennifer L,
Coggins John R,
Price Nicholas C,
Lapthorn Adrian J
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03346-x
Subject(s) - streptomyces coelicolor , substrate (aquarium) , enzyme , chemistry , mycobacterium tuberculosis , combinatorial chemistry , substrate specificity , stereochemistry , catalysis , biochemistry , biology , tuberculosis , medicine , ecology , pathology , mutant , gene
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.