| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2030003 | Structure | 2008 | 4 Pages |
Abstract
In this issue, Hawse et al. (2008) provide additional insight into the mechanistic properties of sirtuin enzymes by describing the structure of a thio-imidate in the active site of Thermatoga maritima Sir2, which strengthens the proposal that the enzyme directly couples NAD+ and acetyllysine oxygen to form a versatile ADPR-peptidyl-imidate intermediate.
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Authors
Anthony A. Sauve,