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|a 10.1093/jxb/erad065
|2 doi
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|a pubmed24n1178.xml
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|a (DE-627)NLM353672912
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|a (NLM)36861318
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Caubrière, Damien
|e verfasserin
|4 aut
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|a Diversity and roles of cysteine desulfurases in photosynthetic organisms
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 08.06.2023
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|a Date Revised 13.06.2023
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a As sulfur is part of many essential protein cofactors such as iron-sulfur clusters, molybdenum cofactors, or lipoic acid, its mobilization from cysteine represents a fundamental process. The abstraction of the sulfur atom from cysteine is catalysed by highly conserved pyridoxal 5'-phosphate-dependent enzymes called cysteine desulfurases. The desulfuration of cysteine leads to the formation of a persulfide group on a conserved catalytic cysteine and the concomitant release of alanine. Sulfur is then transferred from cysteine desulfurases to different targets. Numerous studies have focused on cysteine desulfurases as sulfur-extracting enzymes for iron-sulfur cluster synthesis in mitochondria and chloroplasts but also for molybdenum cofactor sulfuration in the cytosol. Despite this, knowledge about the involvement of cysteine desulfurases in other pathways is quite rudimentary, particularly in photosynthetic organisms. In this review, we summarize current understanding of the different groups of cysteine desulfurases and their characteristics in terms of primary sequence, protein domain architecture, and subcellular localization. In addition, we review the roles of cysteine desulfurases in different fundamental pathways and highlight the gaps in our knowledge to encourage future work on unresolved issues especially in photosynthetic organisms
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|a Review
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Cysteine
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|a cysteine desulfurase
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|a iron–sulfur cluster
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|a molybdenum cofactor
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|a persulfide group
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|a sulfur trafficking
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|a cysteine desulfurase
|2 NLM
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|a EC 4.4.1.-
|2 NLM
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|a Cysteine
|2 NLM
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|a K848JZ4886
|2 NLM
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|a Carbon-Sulfur Lyases
|2 NLM
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|a EC 4.4.-
|2 NLM
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|a Pyridoxal Phosphate
|2 NLM
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|a 5V5IOJ8338
|2 NLM
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|a Sulfur
|2 NLM
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|a 70FD1KFU70
|2 NLM
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|a Iron
|2 NLM
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|a E1UOL152H7
|2 NLM
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|a Iron-Sulfur Proteins
|2 NLM
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|a Moseler, Anna
|e verfasserin
|4 aut
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1 |
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|a Rouhier, Nicolas
|e verfasserin
|4 aut
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|a Couturier, Jérémy
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 74(2023), 11 vom: 06. Juni, Seite 3345-3360
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:74
|g year:2023
|g number:11
|g day:06
|g month:06
|g pages:3345-3360
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|u http://dx.doi.org/10.1093/jxb/erad065
|3 Volltext
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|a GBV_ILN_350
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|a AR
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|d 74
|j 2023
|e 11
|b 06
|c 06
|h 3345-3360
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