The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
GCN5-Related N-Acetyltransferases: A Structural Overview
Open accessAbstract
Hundreds of acetyltransferases exist. All use a common acetyl donor--acetyl coenzyme A--and each exhibits remarkable specificity for acetyl acceptors, which include small molecules and proteins. Analysis of the primary sequences of these enzymes indicates that they can be sorted into several superfamilies. This review covers the three-dimensional structures of members of one of these superfamilies, now referred to in the literature as the GCN5-related N-acetyltransferases (GNAT), reflecting the importance of one functional category, the histone acetyltransferases. Despite the diversity of substrate specificities, members of the GNAT superfamily demonstrate remarkable similarity in protein topology and mode of acetyl coenzyme A binding, likely reflecting a conserved catalytic mechanism.
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Metadata
- Authors
- Dyda, F., Klein, D. C., & Hickman, A. B.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2000-06
- Volume
- 29
- Issue
- 1
- Pages
- 81-103
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2111199460
- Cited by
- 455
- References
- 39
- FWCI
- 3.27
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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