What question did this study set out to answer?

To review the biochemical mechanisms, structural features, and biological functions of protein lysine acetylation catalyzed by the paralogous acetyltransferases p300 and CBP.

January 16, 2015Chemical ReviewsOpen Access

Protein Lysine Acetylation by p300/CBP

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To review the biochemical mechanisms, structural features, and biological functions of protein lysine acetylation catalyzed by the paralogous acetyltransferases p300 and CBP.
Literature review analyzing structural, biochemical, and functional characterizations of p300/CBP acetyltransferases.
Evaluation of catalytic mechanisms, cellular substrate repertoires, and chemical inhibitors targeting the p300/CBP catalytic core.
p300 and CBP function as broadly acting transcriptional coactivators that catalyze lysine acetylation across histones and numerous non-histone regulatory proteins.
Structural and kinetic insights define distinct catalytic mechanisms and autoregulatory loops that dictate substrate specificity and enzymatic turnover.
Dysregulation of p300/CBP activity contributes to oncogenesis, developmental disorders, and metabolic diseases, identifying these enzymes as tractable drug targets.

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Implication

Review details the catalytic mechanisms and regulatory roles of p300 and CBP in lysine acetylation, highlighting therapeutic opportunities for acetyltransferase inhibitors.

Cite This Study

Dancy et al. (2015) studied this question.

synapsesocial.com/papers/6a1cd8cdc9d372840a89c7ff https://doi.org/10.1021/cr500452k

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Implication

Review details the catalytic mechanisms and regulatory roles of p300 and CBP in lysine acetylation, highlighting therapeutic opportunities for acetyltransferase inhibitors.

Protein Lysine Acetylation by p300/CBP

Key Points

Discussion

Implication

Cite This Study

Protein Lysine Acetylation by p300/CBP

Key Points

Discussion

Implication

Cite This Study

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