. Author manuscript; available in PMC: 2018 Jan 20.

Published in final edited form as: ACS Chem Biol. 2016 Dec 20;12(1):300–310. doi: 10.1021/acschembio.6b00954

Table 4.

Summary of SIRT7 WT and mutants’ activities and RNA-binding affinities in the presence of 5S rRNA

SIRT7	K_d (nM)	Relative Deacetylation (H3K18 Ac)	Relative Demyristoylation (H3K9 Myr)	Fraction of SIRT7 bound with 5SRNA in the assay ^**
WT	81 ± 5	1.00	1.00	0.98
M1^*	520 ± 130	0.45	0.31	0.89
M2	1600 ± 250	1.06	0.69	0.74
M3^*	3000 ± 570	0.23	0.40	0.62
M4^*	4200 ± 600	0.28	0.47	0.54
M5	3800 ± 230	1.22	0.74	0.56
M6	4000 ± 1500	1.74	1.00	0.55
M7^*	540 ± 40	0.23	0.17	0.89
M8	1600 ± 50	0.87	0.79	0.74
M9^*	6800 ± 1000	0.00	0.06	0.43

Mutants with flawed catalytic activities (less than 50% of WT SIRT7) in the presence of 5S rRNA. Conversion Rate of WT SIRT7 was set at 1.00, all the mutants’ conversion rates were normalized using that of WT SIRT7.

^**

SIRT7 (2 µM) was incubated with 6 µM of 5S rRNA. The fraction of SIRT7 bound with 5S rRNA was calculated assumpting that one molecule of SIRT7 associates with one molecule of 5S rRNA.