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Structural, functional and evolutionary diversity of 4-coumarate-CoA ligase in plants
Phenylpropanoid pathway provides precursors for numerous secondary metabolites in plants. In this pathway, 4-coumarate-CoA ligase (EC 6.2.1.12, 4CL) is the main branch point enzyme which generates activated thioesters. Being the last enzyme of three shared common steps in general phenylpropanoid pat...
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Published in: | Planta 2018-11, Vol.248 (5), p.1063-1078 |
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description | Phenylpropanoid pathway provides precursors for numerous secondary metabolites in plants. In this pathway, 4-coumarate-CoA ligase (EC 6.2.1.12, 4CL) is the main branch point enzyme which generates activated thioesters. Being the last enzyme of three shared common steps in general phenylpropanoid pathway, it contributes to channelize precursors for different phenylpropanoids. In plants, 4CL enzymes are present in multiple isoforms and encoded by small gene family. It belongs to adenylate-forming enzyme family and catalyzes the reaction that converts hydroxy or methoxy cinnamic acid derivatives to corresponding thioesters. These thioesters are further utilized for biosynthesis of phenylpropanoids, which are known for having numerous nutritional and medicinal applications. In addition, the 4CL enzymes have been characterized from various plants for their role in plant physiology or in biotic and abiotic stresses. Furthermore, specific isoforms are differentially regulated upon exposure to diverse stimuli leading to flux diversion toward the particular metabolite biosynthesis. Evolutionary studies showed that 4CL separately evolved after monocot and dicot segregation. Here, we provide a comprehensive review on 4CL, which includes evolution, function, gene/protein structure, role in metabolite biosynthesis and cellular partition, and their regulation. Based on the available data, we have explored the scope for pathway engineering by utilizing 4CL enzymes. |
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In this pathway, 4-coumarate-CoA ligase (EC 6.2.1.12, 4CL) is the main branch point enzyme which generates activated thioesters. Being the last enzyme of three shared common steps in general phenylpropanoid pathway, it contributes to channelize precursors for different phenylpropanoids. In plants, 4CL enzymes are present in multiple isoforms and encoded by small gene family. It belongs to adenylate-forming enzyme family and catalyzes the reaction that converts hydroxy or methoxy cinnamic acid derivatives to corresponding thioesters. These thioesters are further utilized for biosynthesis of phenylpropanoids, which are known for having numerous nutritional and medicinal applications. In addition, the 4CL enzymes have been characterized from various plants for their role in plant physiology or in biotic and abiotic stresses. Furthermore, specific isoforms are differentially regulated upon exposure to diverse stimuli leading to flux diversion toward the particular metabolite biosynthesis. Evolutionary studies showed that 4CL separately evolved after monocot and dicot segregation. Here, we provide a comprehensive review on 4CL, which includes evolution, function, gene/protein structure, role in metabolite biosynthesis and cellular partition, and their regulation. Based on the available data, we have explored the scope for pathway engineering by utilizing 4CL enzymes.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-018-2965-z</identifier><identifier>PMID: 30078075</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Science + Business Media</publisher><subject>4-Coumarate-CoA ligase ; Abiotic stress ; Agriculture ; biochemical pathways ; Biofuels ; Biomedical and Life Sciences ; Biosynthesis ; Cellular structure ; Cinnamic acid ; coumarate-CoA ligase ; Developmental stages ; Ecology ; Enzymes ; Evolution ; family ; Forestry ; fuel production ; genes ; Isoforms ; Life Sciences ; Liliopsida ; Magnoliopsida ; Metabolic engineering ; Metabolites ; Phenylpropanoids ; Plant physiology ; Plant Sciences ; Plants (botany) ; Precursors ; Protein structure ; Proteins ; Resveratrol ; REVIEW ; Secondary metabolites ; Stresses ; Structure-function relationships ; Thioesters</subject><ispartof>Planta, 2018-11, Vol.248 (5), p.1063-1078</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>Planta is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-6eac087cb725ce175395aadfff54b64409a29f296842990e450cb07f8b1443373</citedby><cites>FETCH-LOGICAL-c493t-6eac087cb725ce175395aadfff54b64409a29f296842990e450cb07f8b1443373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/48727045$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/48727045$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,58213,58446</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30078075$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lavhale, Santosh G.</creatorcontrib><creatorcontrib>Kalunke, Raviraj M.</creatorcontrib><creatorcontrib>Giri, Ashok P.</creatorcontrib><title>Structural, functional and evolutionary diversity of 4-coumarate-CoA ligase in plants</title><title>Planta</title><addtitle>Planta</addtitle><addtitle>Planta</addtitle><description>Phenylpropanoid pathway provides precursors for numerous secondary metabolites in plants. In this pathway, 4-coumarate-CoA ligase (EC 6.2.1.12, 4CL) is the main branch point enzyme which generates activated thioesters. Being the last enzyme of three shared common steps in general phenylpropanoid pathway, it contributes to channelize precursors for different phenylpropanoids. In plants, 4CL enzymes are present in multiple isoforms and encoded by small gene family. It belongs to adenylate-forming enzyme family and catalyzes the reaction that converts hydroxy or methoxy cinnamic acid derivatives to corresponding thioesters. These thioesters are further utilized for biosynthesis of phenylpropanoids, which are known for having numerous nutritional and medicinal applications. In addition, the 4CL enzymes have been characterized from various plants for their role in plant physiology or in biotic and abiotic stresses. Furthermore, specific isoforms are differentially regulated upon exposure to diverse stimuli leading to flux diversion toward the particular metabolite biosynthesis. Evolutionary studies showed that 4CL separately evolved after monocot and dicot segregation. Here, we provide a comprehensive review on 4CL, which includes evolution, function, gene/protein structure, role in metabolite biosynthesis and cellular partition, and their regulation. 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diversity of 4-coumarate-CoA ligase in plants</atitle><jtitle>Planta</jtitle><stitle>Planta</stitle><addtitle>Planta</addtitle><date>2018-11-01</date><risdate>2018</risdate><volume>248</volume><issue>5</issue><spage>1063</spage><epage>1078</epage><pages>1063-1078</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><abstract>Phenylpropanoid pathway provides precursors for numerous secondary metabolites in plants. In this pathway, 4-coumarate-CoA ligase (EC 6.2.1.12, 4CL) is the main branch point enzyme which generates activated thioesters. Being the last enzyme of three shared common steps in general phenylpropanoid pathway, it contributes to channelize precursors for different phenylpropanoids. In plants, 4CL enzymes are present in multiple isoforms and encoded by small gene family. It belongs to adenylate-forming enzyme family and catalyzes the reaction that converts hydroxy or methoxy cinnamic acid derivatives to corresponding thioesters. These thioesters are further utilized for biosynthesis of phenylpropanoids, which are known for having numerous nutritional and medicinal applications. In addition, the 4CL enzymes have been characterized from various plants for their role in plant physiology or in biotic and abiotic stresses. Furthermore, specific isoforms are differentially regulated upon exposure to diverse stimuli leading to flux diversion toward the particular metabolite biosynthesis. Evolutionary studies showed that 4CL separately evolved after monocot and dicot segregation. Here, we provide a comprehensive review on 4CL, which includes evolution, function, gene/protein structure, role in metabolite biosynthesis and cellular partition, and their regulation. Based on the available data, we have explored the scope for pathway engineering by utilizing 4CL enzymes.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Science + Business Media</pub><pmid>30078075</pmid><doi>10.1007/s00425-018-2965-z</doi><tpages>16</tpages></addata></record> |
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subjects | 4-Coumarate-CoA ligase Abiotic stress Agriculture biochemical pathways Biofuels Biomedical and Life Sciences Biosynthesis Cellular structure Cinnamic acid coumarate-CoA ligase Developmental stages Ecology Enzymes Evolution family Forestry fuel production genes Isoforms Life Sciences Liliopsida Magnoliopsida Metabolic engineering Metabolites Phenylpropanoids Plant physiology Plant Sciences Plants (botany) Precursors Protein structure Proteins Resveratrol REVIEW Secondary metabolites Stresses Structure-function relationships Thioesters |
title | Structural, functional and evolutionary diversity of 4-coumarate-CoA ligase in plants |
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