Skip to main content
. Author manuscript; available in PMC: 2016 May 19.
Published in final edited form as: Biochemistry. 2015 May 4;54(19):3037–3050. doi: 10.1021/acs.biochem.5b00150

Figure 2. kcat and Km, NAD for SIRT1, SIRT2, SIRT3, and SIRT6 deacylation reactions.

Figure 2

A, kcat, inset: kcat for acetylated substrate plotted separately for clarity; Calculated kcat values determined from non-linear regression fits to Michaelis-Menten shown below (n ≥ 3, ± standard deviation). *Estimate for SIRT3 resulting from inability to saturate reaction with NAD+. B, Km for NAD+, Calculated Km, NAD values determined from non-linear regression fits to Michaelis-Menten shown below. *Estimate for SIRT3, **Km, NAD with acetylated peptide for SIRT6 was not measured due to prohibitively high peptide substrate necessary to saturate the reaction (n ≥ 3, ± standard deviation of mean).