Abstract | BACKGROUND: FINDINGS: We have performed site-directed mutagenesis, steady-state kinetics, equilibrium binding measurements and molecular modeling for both the wild-type M. tuberculosis shikimate dehydrogenase and the K69A mutant enzymes. The apparent steady-state kinetic parameters for the M. tuberculosis shikimate dehydrogenase were determined; the catalytic constant value for the wild-type enzyme (50 s-1) is 68-fold larger than that for the mutant K69A (0.73 s-1). There was a modest increase in the Michaelis-Menten constant for DHS (K69A = 76 microM; wild-type = 29 microM) and NADPH (K69A = 30 microM; wild-type = 11 microM). The equilibrium dissociation constants for wild-type and K69A mutant enzymes are 32 (+/- 4) microM and 134 (+/- 21), respectively. CONCLUSION:
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Authors | Valnês S Rodrigues Jr, Ardala Breda, Diógenes S Santos, Luiz A Basso |
Journal | BMC research notes
(BMC Res Notes)
Vol. 2
Pg. 227
(Nov 16 2009)
ISSN: 1756-0500 [Electronic] England |
PMID | 19917104
(Publication Type: Journal Article)
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