EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.B43 | D101N |
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+ |
729960 |
| 2.3.1.B43 | F159A |
the Km value of the mutant enzyme is twice that of wild type enzyme, whereas the kcat is 5fold less. In the F159A mutant, two water molecules occupy the position of the Phe159 ring |
729960 |
| 2.3.1.B43 | H158Y |
catalytically inactive |
739069 |
| 2.3.1.B43 | H158Y |
mutation significantly increases the Km for desuccinylation |
730964 |
| 2.3.1.B43 | H158Y |
site-directed mutagenesis, catalytically inactive mutant, method, overview |
757590 |
| 2.3.1.B43 | H158Y |
site-directed mutagenesis, like the wild-type enzyme, mutant SIRT5-H158Y overexpression significantly increases secondary LPS stimulation-induced interleukin-6 and TNF-alpha production in RAW264.7 cells |
757084 |
| 2.3.1.B43 | H80N |
mutant retains about 60% of the NAD binding ability of wild type Sir2 |
729960 |
| 2.3.1.B43 | more |
CRISPR (clustered regularly interspaced short palindromic repeats) is used to delete SIRT5 in human cell line HEK-293 |
757175 |
| 2.3.1.B43 | more |
generation of SIRT5 deletion mutant mice, homogenates prepared from whole SIRT5-/- liver show reduced Complex II-driven respiration. The enzymatic activities of Complex II and ATP synthase are also significantly reduced |
757175 |
| 2.3.1.B43 | more |
generation of SIRT5 knockout mice on the Sv129 background using the lentiviral SIRT5 shRNA plasmid sc-63027-SH |
756555 |
