The cysteine regulatory complex from plants and microbes: what was old is new again
- PMID: 23510784
- DOI: 10.1016/j.sbi.2013.02.011
The cysteine regulatory complex from plants and microbes: what was old is new again
Abstract
The physical organization of enzymes in metabolism is an old concept being revisited by new experimental approaches. In plants and microbes, the enzymes of cysteine biosynthesis-serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS)-form a bi-enzyme complex called the cysteine regulatory complex (CRC), which likely plays a role in modulating cysteine biosynthesis in response to sulfur nutrient state. Structural and biochemical studies of SAT and OASS as individual enzymes and recent advances in structural, biophysical, and in vivo analysis of the CRC provide new insights on the function of this macromolecular assembly in plants and microbes and opens biotechnology and pharmaceutical opportunities for future exploration.
Copyright © 2013 Elsevier Ltd. All rights reserved.
Similar articles
-
Two Distinct Assembly States of the Cysteine Regulatory Complex of Salmonella typhimurium Are Regulated by Enzyme-Substrate Cognate Pairs.Biochemistry. 2017 May 9;56(18):2385-2399. doi: 10.1021/acs.biochem.6b01204. Epub 2017 Apr 21. Biochemistry. 2017. PMID: 28414426
-
Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex.Plant Cell. 2006 Dec;18(12):3647-55. doi: 10.1105/tpc.106.047316. Epub 2006 Dec 28. Plant Cell. 2006. PMID: 17194764 Free PMC article.
-
A mechanistic model of the cysteine synthase complex.J Mol Biol. 2009 Feb 13;386(1):37-59. doi: 10.1016/j.jmb.2008.08.075. Epub 2008 Sep 5. J Mol Biol. 2009. PMID: 18801369
-
Advancements in inhibitors of crucial enzymes in the cysteine biosynthetic pathway: Serine acetyltransferase and O-acetylserine sulfhydrylase.Chem Biol Drug Des. 2024 Jul;104(1):e14573. doi: 10.1111/cbdd.14573. Chem Biol Drug Des. 2024. PMID: 38965664 Review.
-
Functional analysis of the cysteine synthase protein complex from plants: structural, biochemical and regulatory properties.J Plant Physiol. 2006 Feb;163(3):273-86. doi: 10.1016/j.jplph.2005.11.013. Epub 2005 Dec 28. J Plant Physiol. 2006. PMID: 16386330 Review.
Cited by
-
Gene identification, expression analysis, and molecular docking of SAT and OASTL in the metabolic pathway of selenium in Cardamine hupingshanensis.Plant Cell Rep. 2024 May 22;43(6):148. doi: 10.1007/s00299-024-03227-6. Plant Cell Rep. 2024. PMID: 38775862 Free PMC article.
-
Proline, Cysteine and Branched-Chain Amino Acids in Abiotic Stress Response of Land Plants and Microalgae.Plants (Basel). 2023 Sep 28;12(19):3410. doi: 10.3390/plants12193410. Plants (Basel). 2023. PMID: 37836150 Free PMC article. Review.
-
Functional characterization of the Serine acetyltransferase family genes uncovers the diversification and conservation of cysteine biosynthesis in tomato.Front Plant Sci. 2022 Sep 21;13:913856. doi: 10.3389/fpls.2022.913856. eCollection 2022. Front Plant Sci. 2022. PMID: 36212318 Free PMC article.
-
The Interplay between Hydrogen Sulfide and Phytohormone Signaling Pathways under Challenging Environments.Int J Mol Sci. 2022 Apr 12;23(8):4272. doi: 10.3390/ijms23084272. Int J Mol Sci. 2022. PMID: 35457090 Free PMC article. Review.
-
Genome-Wide Investigation of the Cysteine Synthase Gene Family Shows That Overexpression of CSase Confers Alkali Tolerance to Alfalfa (Medicago sativa L.).Front Plant Sci. 2022 Jan 4;12:792862. doi: 10.3389/fpls.2021.792862. eCollection 2021. Front Plant Sci. 2022. PMID: 35058952 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials