| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8291618 | Archives of Biochemistry and Biophysics | 2011 | 8 Pages |
Abstract
⺠This study describes for the first time the catalytic mechanism and cofactor preference of an antibiotic target, MRSA-DHDPR. ⺠MRSA-DHDPR follows a compulsory order ternary complex kinetic mechanism. ⺠MRSA-DHDPR binds with 20-fold greater affinity to NADPH compared to NADH. ⺠However, MRSA-DHDPR shows substrate (DHDP) inhibition when utilizing NADPH as the cofactor. ⺠These findings provide insight into rational drug design strategies targeting MRSA-DHDPR.
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Authors
Sudhir R. Dommaraju, Con Dogovski, Peter E. Czabotar, Lilian Hor, Brian J. Smith, Matthew A. Perugini,