GMP Synthetase: Allostery, Structure, and Function Article Swipe
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· 2023
· Open Access
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· DOI: https://doi.org/10.3390/biom13091379
Glutamine amidotransferases (GATs) catalyze the hydrolysis of glutamine and transfer the generated ammonia to diverse metabolites. The two catalytic activities, glutaminolysis and the subsequent amination of the acceptor substrate, happen in two distinct catalytic pockets connected by a channel that facilitates the movement of ammonia. The de novo pathway for the synthesis of guanosine monophosphate (GMP) from xanthosine monophosphate (XMP) is enabled by the GAT GMP synthetase (GMPS). In most available crystal structures of GATs, the ammonia channel is evident in their native state or upon ligand binding, providing molecular details of the conduit. In addition, conformational changes that enable the coordination of the two catalytic chemistries are also informed by the available structures. In contrast, despite the first structure of a GMPS being published in 1996, the understanding of catalysis in the acceptor domain and inter-domain crosstalk became possible only after the structure of a glutamine-bound mutant of Plasmodium falciparum GMPS was determined. In this review, we present the current status of our understanding of the molecular basis of catalysis in GMPS, becoming the first comprehensive assessment of the biochemical function of this intriguing enzyme.
Related Topics
- Type
- review
- Language
- en
- Landing Page
- https://doi.org/10.3390/biom13091379
- https://www.mdpi.com/2218-273X/13/9/1379/pdf?version=1694498702
- OA Status
- gold
- Cited By
- 11
- References
- 68
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4386638162
Raw OpenAlex JSON
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https://openalex.org/W4386638162Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.3390/biom13091379Digital Object Identifier
- Title
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GMP Synthetase: Allostery, Structure, and FunctionWork title
- Type
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reviewOpenAlex work type
- Language
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enPrimary language
- Publication year
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2023Year of publication
- Publication date
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2023-09-12Full publication date if available
- Authors
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Lionel Ballut, Sébastien Violot, Sanjeev Kumar, N. Aghajari, Hemalatha BalaramList of authors in order
- Landing page
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https://doi.org/10.3390/biom13091379Publisher landing page
- PDF URL
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https://www.mdpi.com/2218-273X/13/9/1379/pdf?version=1694498702Direct link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
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goldOpen access status per OpenAlex
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https://www.mdpi.com/2218-273X/13/9/1379/pdf?version=1694498702Direct OA link when available
- Concepts
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Allosteric regulation, Chemistry, Adenylylation, Amination, Guanosine, Biochemistry, Enzyme, Combinatorial chemistry, Catalysis, BiosynthesisTop concepts (fields/topics) attached by OpenAlex
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11Total citation count in OpenAlex
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2025: 8, 2024: 3Per-year citation counts (last 5 years)
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68Number of works referenced by this work
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-
10Other works algorithmically related by OpenAlex
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