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Cited by 166

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A Sphingolipid Desaturase from Higher Plants

Open access
Sperling, Petra, Zähringer, Ulrich, Heinz, Ernst·1998·Journal of Biological Chemistry

Abstract

A recently cloned cDNA from sunflower codes for a fusion protein composed of an N-terminal cytochrome b5 and a domain similar to membrane-bound acyl lipid desaturases. For a functional identification, homologous cDNAs from Brassica napus and Arabidopsis thaliana were expressed in Saccharomyces cerevisiae, and sphingolipid long chain bases were analyzed. The expression of the heterologous enzyme results in significant proportions of new Delta8, 9-cis/trans-phytosphingenines that accompany the residual C18-phytosphinganine predominating in wild-type yeast cells. These results represent the first identification of a gene coding for a sphingolipid desaturase and for a stereounselective desaturase showing trans-activity from any organism. Furthermore, this fusion protein is a new member of the cytochrome b5 superfamily. The formation of the two regioisomeric phytosphingenines in the transformed yeast sheds new light on the factors controlling regioselectivity.

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Metadata

Authors
Sperling, P., Zähringer, U., & Heinz, E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-11
Volume
273
Issue
44
Pages
28590-28596
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1969211270
Cited by
166
References
0
FWCI
3.04
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A Sphingolipid Desaturase from Higher Plants. https://app.cochat.ai/papers/10.1074/jbc.273.44.28590
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Sperling, P., Zähringer, U., & Heinz, E. (1998). A Sphingolipid Desaturase from Higher Plants. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.44.28590

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.