Current Advancements in Sactipeptide Natural Products

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Des...
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Autor*in:	Yunliang Chen [verfasserIn] Jinxiu Wang [verfasserIn] Guoquan Li [verfasserIn] Yunpeng Yang [verfasserIn] Wei Ding [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme

Übergeordnetes Werk:	In: Frontiers in Chemistry - Frontiers Media S.A., 2014, 9(2021)
Übergeordnetes Werk:	volume:9 ; year:2021

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fchem.2021.595991

Katalog-ID:	DOAJ058740562

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520			\|a Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides.
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allfields_unstemmed	10.3389/fchem.2021.595991 doi (DE-627)DOAJ058740562 (DE-599)DOAJ10552e27102a4e958ab17bf67e3af317 DE-627 ger DE-627 rakwb eng QD1-999 Yunliang Chen verfasserin aut Current Advancements in Sactipeptide Natural Products 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides. sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme Chemistry Yunliang Chen verfasserin aut Jinxiu Wang verfasserin aut Guoquan Li verfasserin aut Yunpeng Yang verfasserin aut Wei Ding verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 9(2021) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:9 year:2021 https://doi.org/10.3389/fchem.2021.595991 kostenfrei https://doaj.org/article/10552e27102a4e958ab17bf67e3af317 kostenfrei https://www.frontiersin.org/articles/10.3389/fchem.2021.595991/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2021
allfieldsGer	10.3389/fchem.2021.595991 doi (DE-627)DOAJ058740562 (DE-599)DOAJ10552e27102a4e958ab17bf67e3af317 DE-627 ger DE-627 rakwb eng QD1-999 Yunliang Chen verfasserin aut Current Advancements in Sactipeptide Natural Products 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides. sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme Chemistry Yunliang Chen verfasserin aut Jinxiu Wang verfasserin aut Guoquan Li verfasserin aut Yunpeng Yang verfasserin aut Wei Ding verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 9(2021) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:9 year:2021 https://doi.org/10.3389/fchem.2021.595991 kostenfrei https://doaj.org/article/10552e27102a4e958ab17bf67e3af317 kostenfrei https://www.frontiersin.org/articles/10.3389/fchem.2021.595991/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2021
allfieldsSound	10.3389/fchem.2021.595991 doi (DE-627)DOAJ058740562 (DE-599)DOAJ10552e27102a4e958ab17bf67e3af317 DE-627 ger DE-627 rakwb eng QD1-999 Yunliang Chen verfasserin aut Current Advancements in Sactipeptide Natural Products 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides. sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme Chemistry Yunliang Chen verfasserin aut Jinxiu Wang verfasserin aut Guoquan Li verfasserin aut Yunpeng Yang verfasserin aut Wei Ding verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 9(2021) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:9 year:2021 https://doi.org/10.3389/fchem.2021.595991 kostenfrei https://doaj.org/article/10552e27102a4e958ab17bf67e3af317 kostenfrei https://www.frontiersin.org/articles/10.3389/fchem.2021.595991/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2021
language	English
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topic_facet	sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme Chemistry
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container_title	Frontiers in Chemistry
authorswithroles_txt_mv	Yunliang Chen @@aut@@ Jinxiu Wang @@aut@@ Guoquan Li @@aut@@ Yunpeng Yang @@aut@@ Wei Ding @@aut@@
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author	Yunliang Chen
spellingShingle	Yunliang Chen misc QD1-999 misc sactipeptide misc antibaceterial misc thioether misc RiPPs: ribosomally produced and post-translationally modified peptides misc SAM radical enzyme misc Chemistry Current Advancements in Sactipeptide Natural Products
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topic_title	QD1-999 Current Advancements in Sactipeptide Natural Products sactipeptide antibaceterial thioether RiPPs: ribosomally produced and post-translationally modified peptides SAM radical enzyme
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title	Current Advancements in Sactipeptide Natural Products
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title_sort	current advancements in sactipeptide natural products
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abstract	Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides.
abstractGer	Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides.
abstract_unstemmed	Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that benefited from genome sequencing technology in the past two decades. RiPPs are widely distributed in nature and show diverse chemical structures and rich biological activities. Despite the various structural characteristic of RiPPs, they follow a common biosynthetic logic: a precursor peptide containing an N-terminal leader peptide and a C-terminal core peptide; in some cases,a follower peptide is after the core peptide. The precursor peptide undergoes a series of modification, transport, and cleavage steps to form a mature natural product with specific activities. Sactipeptides (Sulfur-to-alpha carbon thioether cross-linked peptides) belong to RiPPs that show various biological activities such as antibacterial, spermicidal and hemolytic properties. Their common hallmark is an intramolecular thioether bond that crosslinks the sulfur atom of a cysteine residue to the α-carbon of an acceptor amino acid, which is catalyzed by a rSAM enzyme. This review summarizes recent achievements concerning the discovery, distribution, structural elucidation, biosynthesis and application prospects of sactipeptides.
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title_short	Current Advancements in Sactipeptide Natural Products
url	https://doi.org/10.3389/fchem.2021.595991 https://doaj.org/article/10552e27102a4e958ab17bf67e3af317 https://www.frontiersin.org/articles/10.3389/fchem.2021.595991/full https://doaj.org/toc/2296-2646
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