Structure Determination of Kahalalide Analogues Based on Metagenomic Analysis of a Bryopsis sp. Marine Green Alga
Two kahalalide analogues were isolated from a sp. marine green alga. Even though our initial structure determination of the peptides by NMR and MS identified them as kahalalide Z (KZ ; ) and Z (KZ ; ), the absolute configuration of the Thr residues by Marfey's analysis was different from those...
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| Veröffentlicht in: | Journal of natural products (Washington, D.C.) D.C.), 2023-11, Vol.86 (11), p.2539-2545 |
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| container_title | Journal of natural products (Washington, D.C.) |
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| creator | Yamazaki, Yuki Yamabe, Sota Komori, Shunnosuke Yoshitake, Kazutoshi Fukuoka, Masashi Sato, Shigeru Takada, Kentaro |
| description | Two kahalalide analogues were isolated from a
sp. marine green alga. Even though our initial structure determination of the peptides by NMR and MS identified them as kahalalide Z
(KZ
;
) and Z
(KZ
;
), the absolute configuration of the Thr residues by Marfey's analysis was different from those found in kahalalide F (KF),
, and
. To ascertain the absolute configuration of the amino acid residues genetically, we conducted a metagenomic analysis for symbiotic bacteria in the alga, leading to the biosynthetic gene cluster (BGC) responsible for producing the kahalalides named kahalalides Z
(KZ
;
) and Z
(KZ
;
). The identification of amino acid residues based on the A-domain suggested these peptides possess the amino acid sequence d-
-Thr-l-Val-l-Val-d-Val residues at the N-terminus, instead of the d-Val-l-Thr-l-Val-d-Val residues found in KF,
, and
. The N-terminal amino acid sequence including absolute configuration was unambiguously determined by a comparison of LCMS data of synthetic tetrapeptides and the hydrolysates derived from
and
. This structural difference is caused by swapping the substrate specificities of the first two A-domains. |
| doi_str_mv | 10.1021/acs.jnatprod.3c00760 |
| format | Article |
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sp. marine green alga. Even though our initial structure determination of the peptides by NMR and MS identified them as kahalalide Z
(KZ
;
) and Z
(KZ
;
), the absolute configuration of the Thr residues by Marfey's analysis was different from those found in kahalalide F (KF),
, and
. To ascertain the absolute configuration of the amino acid residues genetically, we conducted a metagenomic analysis for symbiotic bacteria in the alga, leading to the biosynthetic gene cluster (BGC) responsible for producing the kahalalides named kahalalides Z
(KZ
;
) and Z
(KZ
;
). The identification of amino acid residues based on the A-domain suggested these peptides possess the amino acid sequence d-
-Thr-l-Val-l-Val-d-Val residues at the N-terminus, instead of the d-Val-l-Thr-l-Val-d-Val residues found in KF,
, and
. The N-terminal amino acid sequence including absolute configuration was unambiguously determined by a comparison of LCMS data of synthetic tetrapeptides and the hydrolysates derived from
and
. This structural difference is caused by swapping the substrate specificities of the first two A-domains.</description><identifier>ISSN: 0163-3864</identifier><identifier>EISSN: 1520-6025</identifier><identifier>DOI: 10.1021/acs.jnatprod.3c00760</identifier><identifier>PMID: 37889636</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Amino Acids ; Animals ; Chlorophyta - chemistry ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Mollusca - chemistry</subject><ispartof>Journal of natural products (Washington, D.C.), 2023-11, Vol.86 (11), p.2539-2545</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c307t-d592ed74cf04da42e85e2e28c6c2a06d8f341ba80d5a63dc9ef6fe01ae749be63</citedby><cites>FETCH-LOGICAL-c307t-d592ed74cf04da42e85e2e28c6c2a06d8f341ba80d5a63dc9ef6fe01ae749be63</cites><orcidid>0000-0003-3835-1482</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2765,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37889636$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamazaki, Yuki</creatorcontrib><creatorcontrib>Yamabe, Sota</creatorcontrib><creatorcontrib>Komori, Shunnosuke</creatorcontrib><creatorcontrib>Yoshitake, Kazutoshi</creatorcontrib><creatorcontrib>Fukuoka, Masashi</creatorcontrib><creatorcontrib>Sato, Shigeru</creatorcontrib><creatorcontrib>Takada, Kentaro</creatorcontrib><title>Structure Determination of Kahalalide Analogues Based on Metagenomic Analysis of a Bryopsis sp. Marine Green Alga</title><title>Journal of natural products (Washington, D.C.)</title><addtitle>J Nat Prod</addtitle><description>Two kahalalide analogues were isolated from a
sp. marine green alga. Even though our initial structure determination of the peptides by NMR and MS identified them as kahalalide Z
(KZ
;
) and Z
(KZ
;
), the absolute configuration of the Thr residues by Marfey's analysis was different from those found in kahalalide F (KF),
, and
. To ascertain the absolute configuration of the amino acid residues genetically, we conducted a metagenomic analysis for symbiotic bacteria in the alga, leading to the biosynthetic gene cluster (BGC) responsible for producing the kahalalides named kahalalides Z
(KZ
;
) and Z
(KZ
;
). The identification of amino acid residues based on the A-domain suggested these peptides possess the amino acid sequence d-
-Thr-l-Val-l-Val-d-Val residues at the N-terminus, instead of the d-Val-l-Thr-l-Val-d-Val residues found in KF,
, and
. The N-terminal amino acid sequence including absolute configuration was unambiguously determined by a comparison of LCMS data of synthetic tetrapeptides and the hydrolysates derived from
and
. This structural difference is caused by swapping the substrate specificities of the first two A-domains.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids</subject><subject>Animals</subject><subject>Chlorophyta - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Structure</subject><subject>Mollusca - chemistry</subject><issn>0163-3864</issn><issn>1520-6025</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtPwzAQhC0EoqXwDxDykUvKxk4c59jyKIhWHIBztLU3JVUerZ0c-u9JactptdqZ2dHH2G0I4xBE-IDGj9c1thvX2LE0AImCMzYMYwGBAhGfsyGESgZSq2jArrxfA4CENL5kA5lonSqphmz72brOtJ0j_kQtuaroI4um5k3O3_EHSywLS3xSY9msOvJ8ip4s7wULanFFdVMV5u-884Xfu5BP3a7Z7De_GfMFuqImPnNENZ-UK7xmFzmWnm6Oc8S-X56_Hl-D-cfs7XEyD4yEpA1snAqySWRyiCxGgnRMgoQ2yggEZXUuo3CJGmyMSlqTUq5yghApidIlKTli94fcHtC2b95mVeENlSXW1HQ-E1rLOJFJFPfS6CA1rvHeUZ5tXFGh22UhZHvYWQ87O8HOjrB7293xQ7esyP6bTnTlLw7kgDs</recordid><startdate>20231124</startdate><enddate>20231124</enddate><creator>Yamazaki, Yuki</creator><creator>Yamabe, Sota</creator><creator>Komori, Shunnosuke</creator><creator>Yoshitake, Kazutoshi</creator><creator>Fukuoka, Masashi</creator><creator>Sato, Shigeru</creator><creator>Takada, Kentaro</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-3835-1482</orcidid></search><sort><creationdate>20231124</creationdate><title>Structure Determination of Kahalalide Analogues Based on Metagenomic Analysis of a Bryopsis sp. Marine Green Alga</title><author>Yamazaki, Yuki ; Yamabe, Sota ; Komori, Shunnosuke ; Yoshitake, Kazutoshi ; Fukuoka, Masashi ; Sato, Shigeru ; Takada, Kentaro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c307t-d592ed74cf04da42e85e2e28c6c2a06d8f341ba80d5a63dc9ef6fe01ae749be63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids</topic><topic>Animals</topic><topic>Chlorophyta - chemistry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Structure</topic><topic>Mollusca - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamazaki, Yuki</creatorcontrib><creatorcontrib>Yamabe, Sota</creatorcontrib><creatorcontrib>Komori, Shunnosuke</creatorcontrib><creatorcontrib>Yoshitake, Kazutoshi</creatorcontrib><creatorcontrib>Fukuoka, Masashi</creatorcontrib><creatorcontrib>Sato, Shigeru</creatorcontrib><creatorcontrib>Takada, Kentaro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of natural products (Washington, D.C.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamazaki, Yuki</au><au>Yamabe, Sota</au><au>Komori, Shunnosuke</au><au>Yoshitake, Kazutoshi</au><au>Fukuoka, Masashi</au><au>Sato, Shigeru</au><au>Takada, Kentaro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure Determination of Kahalalide Analogues Based on Metagenomic Analysis of a Bryopsis sp. Marine Green Alga</atitle><jtitle>Journal of natural products (Washington, D.C.)</jtitle><addtitle>J Nat Prod</addtitle><date>2023-11-24</date><risdate>2023</risdate><volume>86</volume><issue>11</issue><spage>2539</spage><epage>2545</epage><pages>2539-2545</pages><issn>0163-3864</issn><eissn>1520-6025</eissn><abstract>Two kahalalide analogues were isolated from a
sp. marine green alga. Even though our initial structure determination of the peptides by NMR and MS identified them as kahalalide Z
(KZ
;
) and Z
(KZ
;
), the absolute configuration of the Thr residues by Marfey's analysis was different from those found in kahalalide F (KF),
, and
. To ascertain the absolute configuration of the amino acid residues genetically, we conducted a metagenomic analysis for symbiotic bacteria in the alga, leading to the biosynthetic gene cluster (BGC) responsible for producing the kahalalides named kahalalides Z
(KZ
;
) and Z
(KZ
;
). The identification of amino acid residues based on the A-domain suggested these peptides possess the amino acid sequence d-
-Thr-l-Val-l-Val-d-Val residues at the N-terminus, instead of the d-Val-l-Thr-l-Val-d-Val residues found in KF,
, and
. The N-terminal amino acid sequence including absolute configuration was unambiguously determined by a comparison of LCMS data of synthetic tetrapeptides and the hydrolysates derived from
and
. This structural difference is caused by swapping the substrate specificities of the first two A-domains.</abstract><cop>United States</cop><pmid>37889636</pmid><doi>10.1021/acs.jnatprod.3c00760</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-3835-1482</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0163-3864 |
| ispartof | Journal of natural products (Washington, D.C.), 2023-11, Vol.86 (11), p.2539-2545 |
| issn | 0163-3864 1520-6025 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2883573745 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | Amino Acid Sequence Amino Acids Animals Chlorophyta - chemistry Magnetic Resonance Spectroscopy Molecular Structure Mollusca - chemistry |
| title | Structure Determination of Kahalalide Analogues Based on Metagenomic Analysis of a Bryopsis sp. Marine Green Alga |
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