Title : The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5).

Pub. Date : 2012 Aug 17

PMID : 22767592






8 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 However, human SIRT5 (sirtuin 5), which has been reported to exhibit little deacetylase activity, was recently identified as an NAD-dependent demalonylase and desuccinylase. NAD sirtuin 5 Homo sapiens
2 However, human SIRT5 (sirtuin 5), which has been reported to exhibit little deacetylase activity, was recently identified as an NAD-dependent demalonylase and desuccinylase. NAD sirtuin 5 Homo sapiens
3 Previously, we solved the crystal structure of a SIRT5-succinyl-lysine peptide-NAD complex. succinyl-lysine peptide sirtuin 5 Homo sapiens
4 Previously, we solved the crystal structure of a SIRT5-succinyl-lysine peptide-NAD complex. NAD sirtuin 5 Homo sapiens
5 Here, we present two more structures: a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD. thiosuccinyl peptide sirtuin 5 Homo sapiens
6 Here, we present two more structures: a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD. thiosuccinyl peptide sirtuin 5 Homo sapiens
7 Here, we present two more structures: a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD. NAD sirtuin 5 Homo sapiens
8 Here, we present two more structures: a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD. NAD sirtuin 5 Homo sapiens