کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1927399 | 1536523 | 2006 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis α-isopropylmalate synthase Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis α-isopropylmalate synthase](/preview/png/1927399.png)
Mycobacterium tuberculosis α-isopropylmalate synthase (MtIPMS) is a member of the family of enzymes that catalyze a Claisen-type condensation. In this work we characterized the monovalent and divalent specificity of MtIPMS using steady-state kinetics. The monovalent cation dependence of the kinetic parameters of substrates and divalent metals indicates that K+ is the likely physiological activator. K+ acts most likely as an allosteric activator, and exerts part of its effect through the catalytic divalent metal. The divalent metal specificity of MtIPMS is broad, and Mg2+ and Mn2+ are the metals that cause the highest activation. Interestingly, Zn2+, first assigned as the catalytic metal, inhibits the enzyme with submicromolar affinity. The features of monovalent cation and divalent metal activation, as well as the inhibition by Zn2+ and Cd2+, are discussed in light of the kinetic and structural information available for MtIPMS and other relevant enzymes.
Journal: Archives of Biochemistry and Biophysics - Volume 451, Issue 2, 15 July 2006, Pages 141–148