Structural basis of SIRT2 pre-catalysis NAD+ binding dynamics and mechanism

Nan Zhang; Kah Chee Pow; Lanfang Chen; Hao Quan

doi:10.1039/d5cb00169b

January 1, 2025RSC Chemical BiologyOpen Access

Structural basis of SIRT2 pre-catalysis NAD+ binding dynamics and mechanism

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Key Points

SIRT2 binding dynamics for NAD+ were elucidated, revealing significant insights into its catalytic mechanism.
The study identified six key intermediates with a focus on the NAD+ dynamics, confirming its role in catalysis.
Observational analysis utilized thioacetyl-lysine analogs for capturing structural intermediates during enzymatic reactions.
These findings may enable further understanding of sirtuins, potentially impacting therapeutic approaches for related diseases.

Implication

Observational study reveals NAD+ binding dynamics in sirtuins, suggesting insights into catalytic mechanisms.

Abstract

Sirtuins are an evolutionarily conserved family of NAD⁺-dependent deacylase whose catalytic mechanism remains actively investigated. While previous studies have captured sirtuin reaction intermediates using thioacetyl-lysine analogs, here we report six...

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Cite This Study

Zhang et al. (2025) studied this question.

synapsesocial.com/papers/68bb49cc6d6d5674bccffcd7 https://doi.org/10.1039/d5cb00169b

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Structural basis of SIRT2 pre-catalysis NAD+ binding dynamics and mechanism

Key Points

Implication

Abstract

Discussion

Cite This Study

Structural basis of SIRT2 pre-catalysis NAD+ binding dynamics and mechanism

Key Points

Implication

Abstract

Discussion

Cite This Study

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