A helical lid converts a sulfotransferase to a dehydratase.
Abstract
We report here the crystal structure of retinol dehydratase, an enzyme that catalyzes the synthesis of anhydroretinol. The enzyme is a member of the sulfotransferase superfamily and its crystal structure reveals the insertion of a helical lid into a canonical sulfotransferase fold. Site-directed mutations demonstrate that this inserted lid is necessary for anhydroretinol production but not for sulfonation; thus, insertion of a helical lid can convert a sulfotransferase into a dehydratase.
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Retinol dehydratase, a sulfotransferase, catalyzes conversion of retinol to anhydroretinol via retinyl sulfate.
“Hydroxyl dissociation can also be facilitated by its conjugation with an electron-withdrawing group, for example a sulfo moiety, as occurs catalytically via the enzyme retinol dehydratase. This member of the sulfotransferase family is responsible for the catalytic conversion of retinol into anhydroretinol.172”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [172]
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Lrat-specific domain facilitates Vitamin A metabolism by domain swapping in HRASLS3
Golczak, M., Sears, A. E., Kiser, P. D., & Palczewski, K. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1687 · Cited by 58 · see citing works
- Authors
- Pakhomova, S. V., Kobayashi, M., Buck, J., & Newcomer, M. E.
- Affiliations
- Vanderbilt University (US)
- Cornell University (US)
- Corresponding author
- Marcia E. Newcomer
- Venue
- Nature Structural Biology
- Published
- 2001-05-01
- Volume
- 8
- Issue
- 5
- Pages
- 447-451
- ISSN
- 1072-8368 (ISSN-L)
- OpenAlex
- W1599840191
- Cited by
- 33
- References
- 0
- Citations by year
- 2024: 1 · 2022: 5 · 2021: 1 · 2015: 2 · 2014: 2 · 2013: 1
- FWCI
- 3.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Civil War Book Review (submittedVersion)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Keywords
- enzyme mechanism, sulfonation, site-directed mutagenesis, protein structure-function relationship, vitamin A metabolism
- MeSH terms
- Amino Acid Sequence, Animals, Benzaldehydes, Binding Sites, Hydro-Lyases, Models, Molecular, Molecular Sequence Data, Mutation, Structure-Activity Relationship, Sulfates, Vitamin A, Sulfotransferases, Sequence Alignment, Protein Structure, Secondary, Crystallography, X-Ray, Amino Acid Substitution
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