Enzymes are
proteins that catalyze chemical reactions in biological systems in terms of the
biocatalyze which has the nature of catalysts in general are involved react,
but at the end of the reaction will be retrieved in its original form. Inhibitor is a compound that can inhibit or decrease the rate of reaction
catalyzed by the enzyme. Enzyme
inhibitors itself are divided into two kinds namely
reversible and irreversible inhibitor. The aims of this experiment was to determine the effect of
inhibitors on enzyme
activity seen from the value of Vmax and KM reaction
without inhibitor and with inhibitor. The method used was quantitative
analysis. In this experiment were used sodium succinate as a substrate and sodium citrate as
a inhibitor. The Na-citrate was inhibited reaction catalyzed
by the enzyme succinate dehydrogenase. The value of KM in reaction without inhibitor is 6.754 x 10-2 M, while in reaction with inhibitor is 0.4 M.
So, it can be conclude that addition of inhibitor concentration cause
increasing in KM value but had no effect on the value of Vmax..
Keywords: Enzyme,
Succinate dehydrogenase, Competitive inhibitor
REFERENCES
Redhana,
I W. & Maryam, S. 2003. Penuntun Praktikum Biokimia. Singaraja: IKIP
Negeri Singaraja.
Tika, I N. 2010. Buku Penuntun Praktikum Biokimia.
Singaraja: Universitas Pendidikan Ganesha.
Tika, I N. 2007. Penuntun
Praktikum Biokimia. Singaraja: Universitas Pendidikan Ganesha
Lakewood,
2011. Effects of Inhibitors on Enzyme
Activity. Worthington: Biochemical Corporation.
Sharma, Rakesh. 2012. Enzyme Inhibition and Bioapplications.
India: InTech
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