Visualizing the Chain-Flipping Mechanism in Fatty-Acid Biosynthesis

The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partn...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie (International ed.) Jg. 53; H. 52; S. 14456 - 14461
Hauptverfasser:	Beld, Joris, Cang, Hu, Burkart, Michael D.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Weinheim WILEY-VCH Verlag 22.12.2014 WILEY‐VCH Verlag Wiley Wiley Subscription Services, Inc
Ausgabe:	International ed. in English
Schlagworte:	acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - metabolism BASIC BIOLOGICAL SCIENCES Biosynthesis Carriers Catalysis Catalysts chain-flipping mechanism Chains Chemistry Chemistry, Multidisciplinary E coli Elongation Escherichia coli fatty acid synthase Fatty acids Fatty Acids - biosynthesis Fluorescence Naphthalimides - chemistry Nuclear Magnetic Resonance, Biomolecular Oxadiazoles - chemistry Physical Sciences Protein Interaction Domains and Motifs Proteins Rhodamines - chemistry Science & Technology solvatochromism Solvents - chemistry DOMAIN fatty acids ESCHERICHIA-COLI chain-flipping mechanism SYNTHASE BETA-KETOACYL acyl carrier protein FLUORESCENCE SPECTROSCOPY fatty acid synthase SPINACH DYNAMICS solvatochromism
ISSN:	1433-7851, 1521-3773, 1521-3773
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain‐flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross‐linking probe and solution‐phase NMR spectroscopy. The chain‐flipping mechanism was visualized by single‐molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. Flipping out in style: Protein–protein interactions with the partner protein ketoacyl synthase II (KASII) cause fatty‐acid‐intermediate cargo sequestered by the acyl carrier protein (ACP) to flip from the hydrophobic core of the carrier protein into the active site of the partner protein. Solvatochromic pantetheine probes were used to visualize this event (see picture).
AbstractList	The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross-linking probe and solution-phase NMR spectroscopy. The chain-flipping mechanism was visualized by single-molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain‐flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross‐linking probe and solution‐phase NMR spectroscopy. The chain‐flipping mechanism was visualized by single‐molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. Flipping out in style: Protein–protein interactions with the partner protein ketoacyl synthase II (KASII) cause fatty‐acid‐intermediate cargo sequestered by the acyl carrier protein (ACP) to flip from the hydrophobic core of the carrier protein into the active site of the partner protein. Solvatochromic pantetheine probes were used to visualize this event (see picture). The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross-linking probe and solution-phase NMR spectroscopy. The chain-flipping mechanism was visualized by single-molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. Flipping out in style: Protein-protein interactions with the partner protein ketoacyl synthaseII (KASII) cause fatty-acid-intermediate cargo sequestered by the acyl carrier protein (ACP) to flip from the hydrophobic core of the carrier protein into the active site of the partner protein. Solvatochromic pantetheine probes were used to visualize this event (see picture). In the fatty acid biosynthesis of plants and bacteria, the acyl carrier protein (ACP) is known to sequester elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. In this paper we exploit solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. Addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity is confirmed by demonstration of a dual solvatochromic-crosslinking probe and solution-phase NMR. The chain-flipping mechanism can be visualized by single molecule fluorescent techniques, demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross-linking probe and solution-phase NMR spectroscopy. The chain-flipping mechanism was visualized by single-molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII.The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross-linking probe and solution-phase NMR spectroscopy. The chain-flipping mechanism was visualized by single-molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. In this paper, we exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross-linking probe and solution-phase NMR spectroscopy. Finally, the chain-flipping mechanism was visualized by single-molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII. The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, thus enhancing fluorescence to reveal the elusive chain‐flipping mechanism. This activity was confirmed by the use of a dual solvatochromic cross‐linking probe and solution‐phase NMR spectroscopy. The chain‐flipping mechanism was visualized by single‐molecule fluorescence techniques, thus demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII.
Author	Beld, Joris Cang, Hu Burkart, Michael D.
AuthorAffiliation	a Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA b Waitt Advanced Biophotonics Center, The Salk Institute for Biological Studies, La Jolla, California, USA
AuthorAffiliation_xml	– name: b Waitt Advanced Biophotonics Center, The Salk Institute for Biological Studies, La Jolla, California, USA – name: a Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA
Author_xml	– sequence: 1 givenname: Joris surname: Beld fullname: Beld, Joris organization: Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358 (USA) – sequence: 2 givenname: Hu surname: Cang fullname: Cang, Hu organization: Waitt Advanced Biophotonics Center, The Salk Institute for Biological Studies, La Jolla, California (USA) – sequence: 3 givenname: Michael D. surname: Burkart fullname: Burkart, Michael D. email: mburkart@ucsd.edu organization: Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358 (USA)
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/25354391$$D View this record in MEDLINE/PubMed https://www.osti.gov/servlets/purl/1342736$$D View this record in Osti.gov
BookMark	eNqNkl1rFDEUhoNUbLt666UseiPI1HwncyOsQ3ctbKuCH5chk8l0U2eTdZJR119vtrtdakEqBHI4ed735JzkGBz44C0ATxE8QRDi19o7e4IholAywR-AI8QwKogQ5CDHlJBCSIYOwXGMV5mXEvJH4BAzwigp0RGovrg46M79dv5ynBZ2XC2088W0c6vVJnVuzSLXiMux8-OpTmldTIxrxm9diGufBdHFx-Bhq7ton-z2Efg8Pf1UvSvm72dn1WReGM5LXmAm2wZjVjaQISNgKy3nNanb1rS8rq2oayYlgrxBGmPTWFqWZU4LTnOMLRmBN1vf1VAvbWOsT73u1Kp3S92vVdBO_X3i3UJdhh-KUszyygbPtwYhJqeicSl3Z4L31iSFCMWC8Ay93FXpw_fBxqSWLhrbddrbMESFBNxMngl0P8pJSUsqsu8IvLiDXoWh93lcG4pLTOU19ex2h_vWbt4rA6-2wE9bhzZ3YL2xewxCSCinkskcXdvJ_6crl3RywVdh8ClL6VZq-hBjb1tldud5sq5TCKrNFNTm_6n9_8uykzuym2r_FJS7K7rOru-h1eTi7PS2tthqXUz2116r-2-KCyKY-noxU_Pz2UcCP8zVnPwB1ET5WA
CODEN	ACIEAY
CitedBy_id	crossref_primary_10_1002_ange_201806865 crossref_primary_10_3390_ijms24076864 crossref_primary_10_1021_jacs_4c05509 crossref_primary_10_1042_BCJ20160041 crossref_primary_10_1002_anie_202312476 crossref_primary_10_1002_cbic_201402578 crossref_primary_10_1002_anie_201602614 crossref_primary_10_1002_cbic_202000747 crossref_primary_10_1021_jacs_5b04525 crossref_primary_10_3390_molecules23092213 crossref_primary_10_1073_pnas_2025597118 crossref_primary_10_1038_s41589_019_0301_y crossref_primary_10_1007_s00253_018_8770_6 crossref_primary_10_1042_BCJ20230161 crossref_primary_10_1038_s41598_018_35257_y crossref_primary_10_1038_s42003_021_01838_3 crossref_primary_10_1002_anie_201806865 crossref_primary_10_1002_anie_201804128 crossref_primary_10_1002_1873_3468_13339 crossref_primary_10_1038_s42003_019_0631_z crossref_primary_10_1021_acs_biochem_4c00822 crossref_primary_10_1039_D4SC05499G crossref_primary_10_3390_ijms26189005 crossref_primary_10_1002_ange_202312476 crossref_primary_10_3390_ijms22073317 crossref_primary_10_1074_jbc_M115_648402 crossref_primary_10_1016_j_tet_2016_11_056 crossref_primary_10_1002_ange_201602614 crossref_primary_10_1039_D1SC07256K crossref_primary_10_1007_s10811_016_0875_7 crossref_primary_10_1111_febs_16405 crossref_primary_10_1002_ange_201804128 crossref_primary_10_1016_j_bbagen_2021_129964 crossref_primary_10_1002_aic_16402
Cites_doi	10.1042/BJ20140239 10.1074/jbc.M703454200 10.1038/nature12810 10.1039/B512735A 10.1021/jp407321g 10.1139/O07-109 10.1002/anie.201301215 10.1021/ja804754y 10.1038/nature12679 10.1016/S0021-9258(19)41179-4 10.1039/c2np20062g 10.1016/S0021-9258(18)52372-3 10.1021/bi052062d 10.1039/C3NP70054B 10.1002/(SICI)1521-3757(19980202)110:3<339::AID-ANGE339>3.0.CO;2-F 10.1021/cr00032a005 10.1021/ja505442h 10.1021/bi902176v 10.1016/0584-8539(86)80095-2 10.1021/bi901713r 10.1016/1010-6030(93)85048-D 10.1002/ange.201301215 10.1126/science.1138249 10.1039/P29900000837 10.1016/j.trac.2007.09.003 10.1007/s10811-013-0203-4 10.1016/j.tibtech.2009.11.002 10.1021/cb6003965 10.1002/(SICI)1521-3773(19980216)37:3<325::AID-ANIE325>3.0.CO;2-L 10.1021/ja4042059 10.1074/jbc.M305459200 10.1039/c3np70054b 10.1039/b512735a
ContentType	Journal Article
Copyright	2014 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Copyright_xml	– notice: 2014 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim – notice: 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. – notice: 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
CorporateAuthor	Univ. of California, San Diego, CA (United States)
CorporateAuthor_xml	– name: Univ. of California, San Diego, CA (United States)
DBID	BSCLL AAYXX CITATION 17B 1KM BLEPL DTL EGQ GNMZZ CGR CUY CVF ECM EIF NPM 7TM K9. 7X8 7SR 8BQ 8FD JG9 OIOZB OTOTI 5PM
DOI	10.1002/anie.201408576
DatabaseName	Istex CrossRef Web of Knowledge Index Chemicus Web of Science Core Collection Science Citation Index Expanded Web of Science Primary (SCIE, SSCI & AHCI) Web of Science - Science Citation Index Expanded - 2014 Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Nucleic Acids Abstracts ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic Engineered Materials Abstracts METADEX Technology Research Database Materials Research Database OSTI.GOV - Hybrid OSTI.GOV PubMed Central (Full Participant titles)
DatabaseTitle	CrossRef Web of Science MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest Health & Medical Complete (Alumni) Nucleic Acids Abstracts MEDLINE - Academic Materials Research Database Engineered Materials Abstracts Technology Research Database METADEX
DatabaseTitleList	ProQuest Health & Medical Complete (Alumni) Materials Research Database Web of Science MEDLINE MEDLINE - Academic CrossRef
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 1KM name: Index Chemicus url: https://www.webofscience.com/wos/woscc/search-with-editions?editions=WOS.IC sourceTypes: Enrichment Source Index Database – sequence: 3 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Chemistry
EISSN	1521-3773
Edition	International ed. in English
EndPage	14461
ExternalDocumentID	PMC4425425 1342736 3528868361 25354391 000346485800027 10_1002_anie_201408576 ANIE201408576 ark_67375_WNG_LMGQ30PL_L
Genre	shortCommunication Research Support, U.S. Gov't, Non-P.H.S Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural
GrantInformation_xml	– fundername: NIH funderid: R01GM094924; R01GM095970 – fundername: California Energy Commission funderid: DOE DE‐EE0003373 – fundername: California Energy Commission grantid: CILMSF 500-10-039 – fundername: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) grantid: R01GM094924 – fundername: Rubicon postdoctoral fellowship – fundername: NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA grantid: R01GM094924; R01GM095970 – fundername: DOE; United States Department of Energy (DOE) grantid: DE-EE0003373 – fundername: NIGMS NIH HHS grantid: R01 GM095970 – fundername: NIGMS NIH HHS grantid: R01 GM094924 – fundername: NIGMS NIH HHS grantid: R01GM094924 – fundername: NIGMS NIH HHS grantid: R01GM095970
GroupedDBID	--- -DZ -~X .3N .GA .Y3 05W 0R~ 10A 1L6 1OB 1OC 1ZS 23M 33P 3SF 3WU 4.4 4ZD 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5RE 5VS 66C 6TJ 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHQN AAMNL AANHP AANLZ AAONW AASGY AAXRX AAYCA AAZKR ABCQN ABCUV ABDBF ABEML ABIJN ABJNI ABLJU ABPPZ ABPVW ABUFD ACAHQ ACBWZ ACCZN ACFBH ACGFS ACIWK ACNCT ACPOU ACPRK ACRPL ACSCC ACXBN ACXQS ACYXJ ADBBV ADEOM ADIZJ ADKYN ADMGS ADNMO ADOZA ADXAS ADZMN AEIGN AEIMD AETEA AEUYR AEYWJ AFBPY AFFNX AFFPM AFGKR AFRAH AFWVQ AFZJQ AGQPQ AGYGG AHBTC AHMBA AITYG AIURR AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALVPJ AMBMR AMYDB ATUGU AUFTA AZBYB AZVAB BAFTC BDRZF BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BSCLL BTSUX BY8 CS3 D-E D-F D0L DCZOG DPXWK DR1 DR2 DRFUL DRSTM EBS EJD F00 F01 F04 F5P G-S G.N GNP GODZA H.T H.X HBH HGLYW HHY HHZ HZ~ IX1 J0M JPC KQQ LATKE LAW LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES M53 MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ NNB O66 O9- OIG P2P P2W P2X P4D PQQKQ Q.N Q11 QB0 QRW R.K RNS ROL RX1 RYL SUPJJ TN5 UB1 UPT V2E W8V W99 WBFHL WBKPD WH7 WIB WIH WIK WJL WOHZO WQJ WXSBR WYISQ XG1 XPP XSW XV2 YZZ ZZTAW ~IA ~KM ~WT AAHHS ACCFJ ADZOD AEEZP AEQDE AEUQT AFPWT AIWBW AJBDE ALUQN RWI VQA WRC AAYXX CITATION O8X 17B 1KM BLEPL DTL GROUPED_WOS_SCIENCE_CITATION_INDEX_EXPANDED GROUPED_WOS_WEB_OF_SCIENCE CGR CUY CVF ECM EIF NPM 7TM K9. 7X8 7SR 8BQ 8FD JG9 AAPBV ABHUG ABWRO ACSMX ACXME ADAWD ADDAD AFVGU AGJLS B-7 OIOZB OTOTI 5PM
ID	FETCH-LOGICAL-c6696-258fd2259d051c70f8e66b3bffcf6bbe7bb588106d1a22cde4999be7764de42e3
IEDL.DBID	DRFUL
ISICitedReferencesCount	42
ISICitedReferencesURI	https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=CitingArticles&UT=000346485800027
ISSN	1433-7851 1521-3773
IngestDate	Tue Nov 04 01:46:33 EST 2025 Wed Nov 29 06:12:03 EST 2023 Fri Jul 11 07:10:11 EDT 2025 Fri Jul 11 09:56:54 EDT 2025 Sat Nov 29 15:04:42 EST 2025 Mon Jul 21 05:58:31 EDT 2025 Wed Oct 22 09:28:35 EDT 2025 Fri Dec 05 22:30:47 EST 2025 Tue Nov 18 20:36:05 EST 2025 Sat Nov 29 05:33:25 EST 2025 Wed Jan 22 16:26:31 EST 2025 Tue Nov 11 03:31:17 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	52
Keywords	DOMAIN fatty acids ESCHERICHIA-COLI chain-flipping mechanism SYNTHASE BETA-KETOACYL acyl carrier protein FLUORESCENCE SPECTROSCOPY fatty acid synthase SPINACH DYNAMICS solvatochromism
Language	English
License	http://onlinelibrary.wiley.com/termsAndConditions#vor 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
LinkModel	DirectLink
LogoURL	https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg
MergedId	FETCHMERGED-LOGICAL-c6696-258fd2259d051c70f8e66b3bffcf6bbe7bb588106d1a22cde4999be7764de42e3
Notes	ark:/67375/WNG-LMGQ30PL-L California Energy Commission - No. DOE DE-EE0003373 istex:F98B625171FF6CA00D98E204DDD3BBA6F5104B75 NIH - No. R01GM094924; No. R01GM095970 ArticleID:ANIE201408576 J.B. was supported by a Rubicon postdoctoral fellowship. M.D.B. and J.B. were funded by California Energy Commission CILMSF 500-10-039; DOE DE-EE0003373; NIH R01GM094924; and R01GM095970. We thank J. J. La Clair for fruitful discussions and support, X. Huang and D. J. Lee for training and support with solution protein NMR spectroscopy, and T. L. Foley (NIH) for the plasmid encoding H. sapiens ACP. J.B. was supported by a Rubicon postdoctoral fellowship. M.D.B. and J.B. were funded by California Energy Commission CILMSF 500‐10‐039; DOE DE‐EE0003373; NIH R01GM094924; and R01GM095970. We thank J. J. La Clair for fruitful discussions and support, X. Huang and D. J. Lee for training and support with solution protein NMR spectroscopy, and T. L. Foley (NIH) for the plasmid encoding ACP. H. sapiens NIH RePORTER ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 EE0003373 USDOE Office of Energy Efficiency and Renewable Energy (EERE), Sustainable Transportation Office. Bioenergy Technologies Office
OpenAccessLink	https://www.osti.gov/servlets/purl/1342736
PMID	25354391
PQID	1636824827
PQPubID	946352
PageCount	6
ParticipantIDs	proquest_miscellaneous_1701002571 proquest_miscellaneous_1639494727 proquest_journals_1636824827 pubmed_primary_25354391 crossref_citationtrail_10_1002_anie_201408576 webofscience_primary_000346485800027CitationCount pubmedcentral_primary_oai_pubmedcentral_nih_gov_4425425 crossref_primary_10_1002_anie_201408576 istex_primary_ark_67375_WNG_LMGQ30PL_L osti_scitechconnect_1342736 wiley_primary_10_1002_anie_201408576_ANIE201408576 webofscience_primary_000346485800027
PublicationCentury	2000
PublicationDate	December 22, 2014
PublicationDateYYYYMMDD	2014-12-22
PublicationDate_xml	– month: 12 year: 2014 text: December 22, 2014 day: 22
PublicationDecade	2010
PublicationPlace	Weinheim
PublicationPlace_xml	– name: Weinheim – name: WEINHEIM – name: Germany – name: United States
PublicationTitle	Angewandte Chemie (International ed.)
PublicationTitleAbbrev	ANGEW CHEM INT EDIT
PublicationTitleAlternate	Angew. Chem. Int. Ed
PublicationYear	2014
Publisher	WILEY-VCH Verlag WILEY‐VCH Verlag Wiley Wiley Subscription Services, Inc
Publisher_xml	– name: WILEY-VCH Verlag – name: WILEY‐VCH Verlag – name: Wiley – name: Wiley Subscription Services, Inc
References	C. Nguyen, R. W. Haushalter, D. J. Lee, P. R. L. Markwick, J. Bruegger, G. Caldara-Festin, K. Finzel, D. R. Jackson, F. Ishikawa, B. O'Dowd, J. A. McCammon, S. J. Opella, S.-C. Tsai, M. D. Burkart, Nature 2014, 505, 427-431. A. S. Worthington, M. D. Burkart, Org. Biomol. Chem. 2006, 4, 44-46. P. Wattana-amorn, C. Williams, E. Ploskoń, R. J. Cox, T. J. Simpson, J. Crosby, M. P. Crump, Biochemistry 2010, 49, 2186-2193. A. M. McLean, E. Socher, O. Varnavski, T. B. Clark, B. Imperiali, T. Goodson III, J. Phys. Chem. B 2013, 117, 15935-15942. G. A. Zornetzer, B. G. Fox, J. L. Markley, Biochemistry 2006, 45, 5217-5227. D. A. Hinckley, P. G. Seybold, D. P. Borris, Spectrochim. Acta Part A 1986, 42, 747-754. E. Płoskoń, C. J. Arthur, S. E. Evans, C. Williams, J. Crosby, T. J. Simpson, M. P. Crump, J. Biol. Chem. 2008, 283, 518-528 A. K. Joshi, L. Zhang, V. S. Rangan, S. Smith, J. Biol. Chem. 2003, 278, 33142-33149. A. Mainz, T. L. Religa, R. Sprangers, R. Linser , L. E. Kay, B. Reif, Angew. Chem. Int. Ed. 2013, 52, 8746-8751 J. Beld, E. C. Sonnenschein, C. R. Vickery, J. P. Noel, M. D. Burkart, Nat. Prod. Rep. 2014, 31, 61-108. M. Leibundgut, S. Jenni, C. Frick, N. Ban, Science 2007, 316, 288-290. G. Loving, B. Imperiali, J. Am. Chem. Soc. 2008, 130, 13630-13638 S. Fery-Forgues, J.-P. Fayet, A. Lopez, J. Photochem. Photobiol. A 1993, 70, 229-243. J. Beld, J. L. Blatti, C. Behnke, M. Mendez, M. D. Burkart, J. Appl. Phycol. 2014, 26, 1619-1629. D. M. Byers, H. Gong, Biochem. Cell Biol. 2007, 85, 649-662. G. S. Loving, M. Sainlos, B. Imperiali, Trends Biotechnol. 2010, 28, 73-83. Angew. Chem. 1998, 110, 339-343. G. D'Agnolo, I. S. Rosenfeld, P. R. Vagelos, J. Biol. Chem. 1975, 250, 5289-5294. A. Masoudi, C. R. H. Raetz, P. Zhou, C. W. Pemble IV, Nature 2014, 505, 422-426. A. S. Worthington, H. Rivera, J. W. Torpey, M. D. Alexander, M. D. Burkart, ACS Chem. Biol. 2006, 1, 687-691 J. E. Cronan, Biochem. J. 2014, 460, 157-163. J. Crosby, M. P. Crump, Nat. Prod. Rep. 2012, 29, 1111-1137. C. Reichardt, Chem. Rev. 1994, 94, 2319-2358 M. S. Alexiou, V. Tychopoulos, S. Ghorbanian, J. H. P. Tyman, R. G. Brown, P. I. Brittain, J. Chem. Soc. Perkin Trans. 2 1990, 837-842. F. Ishikawa, R. W. Haushalter, D. J. Lee, K. Finzel, M. D. Burkart, J. Am. Chem. Soc. 2013, 135, 8846-8849. J. J. La Clair, Angew. Chem. Int. Ed. 1998, 37, 325-329 D. Post-Beittenmiller, J. G. Jaworski, J. B. Ohlrogge, J. Biol. Chem. 1991, 266, 1858-1865. D. Pappas, S. M. Burrows, R. D. Reif, TrAC Trends Anal. Chem. 2007, 26, 884-894. M. N. R. Johnson, C. H. Londergan, L. K. Charkoudian, J. Am. Chem. Soc. 2014, 136, 11240-11243. Angew. Chem. 2013, 125, 8909-8914. D. I. Chan, D. P. Tieleman, H. J. Vogel, Biochemistry 2010, 49, 2860-2868. 1975; 250 2014; 26 2006; 4 2006; 1 2003; 278 2014; 136 2008; 283 2013 2013; 52 125 1998 1998; 37 110 2010; 49 2007; 316 2014; 505 1991; 266 2006; 45 1990 1986; 42 2010; 28 1993; 70 2013; 117 2013; 135 2012; 29 2007; 85 1994; 94 2014; 460 2008; 130 2007; 26 2014; 31 e_1_2_2_3_2 e_1_2_2_24_2 e_1_2_2_4_2 e_1_2_2_23_2 e_1_2_2_5_2 e_1_2_2_22_2 e_1_2_2_6_2 e_1_2_2_21_2 e_1_2_2_1_2 e_1_2_2_2_2 Post‐Beittenmiller D. (e_1_2_2_20_2) 1991; 266 e_1_2_2_29_2 e_1_2_2_7_2 e_1_2_2_8_2 e_1_2_2_28_2 e_1_2_2_27_2 e_1_2_2_25_3 e_1_2_2_9_2 e_1_2_2_25_2 e_1_2_2_13_2 e_1_2_2_12_2 e_1_2_2_11_2 e_1_2_2_10_2 e_1_2_2_19_2 e_1_2_2_30_2 e_1_2_2_18_2 e_1_2_2_31_2 e_1_2_2_17_2 e_1_2_2_32_2 e_1_2_2_16_2 e_1_2_2_33_2 e_1_2_2_14_3 e_1_2_2_15_2 e_1_2_2_34_2 e_1_2_2_14_2 D’Agnolo G. (e_1_2_2_26_2) 1975; 250 Pappas, D (WOS:000250846800015) 2007; 26 Crosby, J (WOS:000308659700006) 2012; 29 Cronan, JE (WOS:000336414300002) 2014; 460 Mainz, A. (000346485800027.20) 2013; 125 Beld, J (WOS:000329887500004) 2014; 31 Mainz, A (WOS:000322835700055) 2013; 52 McLean, AM (WOS:000328920600003) 2013; 117 REICHARDT, C (WOS:A1994PY50400005) 1994; 94 ALEXIOU, MS (WOS:A1990DD96000029) 1990 Ploskon, E (WOS:000251940300057) 2008; 283 Zornetzer, GA (WOS:000237049400014) 2006; 45 Nguyen, C (WOS:000329621800048) 2014; 505 HINCKLEY, DA (WOS:A1986D018700009) 1986; 42 La Clair, JJ (WOS:000072138500018) 1998; 37 Masoudi, A (WOS:000329621800047) 2014; 505 Loving, G (WOS:000259924000031) 2008; 130 Byers, DM (WOS:000252316300001) 2007; 85 La Clair, J. J. (000346485800027.15) 1998; 110 Moerner, W. E. (000346485800027.23) 2014 Johnson, MNR (WOS:000340442700009) 2014; 136 POSTBEITTENMILLER, D (WOS:A1991EU49700075) 1991; 266 Ishikawa, F (WOS:000320899200021) 2013; 135 Wattana-Amorn, P (WOS:000275227000011) 2010; 49 DAGNOLO, G (WOS:A1975AK27200002) 1975; 250 Chan, DI (WOS:000275978900012) 2010; 49 Leibundgut, M (WOS:000245654500054) 2007; 316 Beld, J (WOS:000340101100001) 2014; 26 Worthington, AS (WOS:000243895300013) 2006; 1 Worthington, AS (WOS:000233968100008) 2006; 4 Loving, GS (WOS:000274556900003) 2010; 28 Joshi, AK (WOS:000184901800080) 2003; 278
References_xml	– reference: D. I. Chan, D. P. Tieleman, H. J. Vogel, Biochemistry 2010, 49, 2860-2868. – reference: C. Reichardt, Chem. Rev. 1994, 94, 2319-2358; – reference: A. M. McLean, E. Socher, O. Varnavski, T. B. Clark, B. Imperiali, T. Goodson III, J. Phys. Chem. B 2013, 117, 15935-15942. – reference: S. Fery-Forgues, J.-P. Fayet, A. Lopez, J. Photochem. Photobiol. A 1993, 70, 229-243. – reference: M. S. Alexiou, V. Tychopoulos, S. Ghorbanian, J. H. P. Tyman, R. G. Brown, P. I. Brittain, J. Chem. Soc. Perkin Trans. 2 1990, 837-842. – reference: D. A. Hinckley, P. G. Seybold, D. P. Borris, Spectrochim. Acta Part A 1986, 42, 747-754. – reference: F. Ishikawa, R. W. Haushalter, D. J. Lee, K. Finzel, M. D. Burkart, J. Am. Chem. Soc. 2013, 135, 8846-8849. – reference: M. N. R. Johnson, C. H. Londergan, L. K. Charkoudian, J. Am. Chem. Soc. 2014, 136, 11240-11243. – reference: D. Pappas, S. M. Burrows, R. D. Reif, TrAC Trends Anal. Chem. 2007, 26, 884-894. – reference: A. S. Worthington, M. D. Burkart, Org. Biomol. Chem. 2006, 4, 44-46. – reference: P. Wattana-amorn, C. Williams, E. Ploskoń, R. J. Cox, T. J. Simpson, J. Crosby, M. P. Crump, Biochemistry 2010, 49, 2186-2193. – reference: Angew. Chem. 1998, 110, 339-343. – reference: A. Mainz, T. L. Religa, R. Sprangers, R. Linser , L. E. Kay, B. Reif, Angew. Chem. Int. Ed. 2013, 52, 8746-8751; – reference: D. M. Byers, H. Gong, Biochem. Cell Biol. 2007, 85, 649-662. – reference: E. Płoskoń, C. J. Arthur, S. E. Evans, C. Williams, J. Crosby, T. J. Simpson, M. P. Crump, J. Biol. Chem. 2008, 283, 518-528; – reference: G. S. Loving, M. Sainlos, B. Imperiali, Trends Biotechnol. 2010, 28, 73-83. – reference: D. Post-Beittenmiller, J. G. Jaworski, J. B. Ohlrogge, J. Biol. Chem. 1991, 266, 1858-1865. – reference: G. D'Agnolo, I. S. Rosenfeld, P. R. Vagelos, J. Biol. Chem. 1975, 250, 5289-5294. – reference: G. A. Zornetzer, B. G. Fox, J. L. Markley, Biochemistry 2006, 45, 5217-5227. – reference: A. Masoudi, C. R. H. Raetz, P. Zhou, C. W. Pemble IV, Nature 2014, 505, 422-426. – reference: J. E. Cronan, Biochem. J. 2014, 460, 157-163. – reference: A. K. Joshi, L. Zhang, V. S. Rangan, S. Smith, J. Biol. Chem. 2003, 278, 33142-33149. – reference: C. Nguyen, R. W. Haushalter, D. J. Lee, P. R. L. Markwick, J. Bruegger, G. Caldara-Festin, K. Finzel, D. R. Jackson, F. Ishikawa, B. O'Dowd, J. A. McCammon, S. J. Opella, S.-C. Tsai, M. D. Burkart, Nature 2014, 505, 427-431. – reference: A. S. Worthington, H. Rivera, J. W. Torpey, M. D. Alexander, M. D. Burkart, ACS Chem. Biol. 2006, 1, 687-691; – reference: J. Beld, J. L. Blatti, C. Behnke, M. Mendez, M. D. Burkart, J. Appl. Phycol. 2014, 26, 1619-1629. – reference: G. Loving, B. Imperiali, J. Am. Chem. Soc. 2008, 130, 13630-13638; – reference: M. Leibundgut, S. Jenni, C. Frick, N. Ban, Science 2007, 316, 288-290. – reference: Angew. Chem. 2013, 125, 8909-8914. – reference: J. Crosby, M. P. Crump, Nat. Prod. Rep. 2012, 29, 1111-1137. – reference: J. J. La Clair, Angew. Chem. Int. Ed. 1998, 37, 325-329; – reference: J. Beld, E. C. Sonnenschein, C. R. Vickery, J. P. Noel, M. D. Burkart, Nat. Prod. Rep. 2014, 31, 61-108. – volume: 136 start-page: 11240 year: 2014 end-page: 11243 publication-title: J. Am. Chem. Soc. – volume: 49 start-page: 2186 year: 2010 end-page: 2193 publication-title: Biochemistry – volume: 94 start-page: 2319 year: 1994 end-page: 2358 publication-title: Chem. Rev. – volume: 4 start-page: 44 year: 2006 end-page: 46 publication-title: Org. Biomol. Chem. – volume: 37 110 start-page: 325 339 year: 1998 1998 end-page: 329 343 publication-title: Angew. Chem. Int. Ed. Angew. Chem. – volume: 130 start-page: 13630 year: 2008 end-page: 13638 publication-title: J. Am. Chem. Soc. – volume: 26 start-page: 884 year: 2007 end-page: 894 publication-title: TrAC Trends Anal. Chem. – volume: 266 start-page: 1858 year: 1991 end-page: 1865 publication-title: J. Biol. Chem. – volume: 70 start-page: 229 year: 1993 end-page: 243 publication-title: J. Photochem. Photobiol. A – volume: 31 start-page: 61 year: 2014 end-page: 108 publication-title: Nat. Prod. Rep. – volume: 505 start-page: 427 year: 2014 end-page: 431 publication-title: Nature – volume: 52 125 start-page: 8746 8909 year: 2013 2013 end-page: 8751 8914 publication-title: Angew. Chem. Int. Ed. Angew. Chem. – volume: 45 start-page: 5217 year: 2006 end-page: 5227 publication-title: Biochemistry – volume: 1 start-page: 687 year: 2006 end-page: 691 publication-title: ACS Chem. Biol. – volume: 250 start-page: 5289 year: 1975 end-page: 5294 publication-title: J. Biol. Chem. – volume: 316 start-page: 288 year: 2007 end-page: 290 publication-title: Science – volume: 26 start-page: 1619 year: 2014 end-page: 1629 publication-title: J. Appl. Phycol. – volume: 42 start-page: 747 year: 1986 end-page: 754 publication-title: Spectrochim. Acta Part A – volume: 135 start-page: 8846 year: 2013 end-page: 8849 publication-title: J. Am. Chem. Soc. – volume: 278 start-page: 33142 year: 2003 end-page: 33149 publication-title: J. Biol. Chem. – volume: 283 start-page: 518 year: 2008 end-page: 528 publication-title: J. Biol. Chem. – volume: 505 start-page: 422 year: 2014 end-page: 426 publication-title: Nature – volume: 49 start-page: 2860 year: 2010 end-page: 2868 publication-title: Biochemistry – volume: 29 start-page: 1111 year: 2012 end-page: 1137 publication-title: Nat. Prod. Rep. – volume: 85 start-page: 649 year: 2007 end-page: 662 publication-title: Biochem. Cell Biol. – start-page: 837 year: 1990 end-page: 842 publication-title: J. Chem. Soc. Perkin Trans. 2 – volume: 460 start-page: 157 year: 2014 end-page: 163 publication-title: Biochem. J. – volume: 28 start-page: 73 year: 2010 end-page: 83 publication-title: Trends Biotechnol. – volume: 117 start-page: 15935 year: 2013 end-page: 15942 publication-title: J. Phys. Chem. B – ident: e_1_2_2_23_2 doi: 10.1042/BJ20140239 – ident: e_1_2_2_7_2 doi: 10.1074/jbc.M703454200 – ident: e_1_2_2_1_2 doi: 10.1038/nature12810 – ident: e_1_2_2_15_2 doi: 10.1039/B512735A – ident: e_1_2_2_33_2 doi: 10.1021/jp407321g – ident: e_1_2_2_2_2 doi: 10.1139/O07-109 – ident: e_1_2_2_25_2 doi: 10.1002/anie.201301215 – ident: e_1_2_2_10_2 doi: 10.1021/ja804754y – ident: e_1_2_2_24_2 doi: 10.1038/nature12679 – volume: 250 start-page: 5289 year: 1975 ident: e_1_2_2_26_2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)41179-4 – ident: e_1_2_2_9_2 – ident: e_1_2_2_3_2 doi: 10.1039/c2np20062g – ident: e_1_2_2_6_2 – volume: 266 start-page: 1858 year: 1991 ident: e_1_2_2_20_2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)52372-3 – ident: e_1_2_2_4_2 doi: 10.1021/bi052062d – ident: e_1_2_2_19_2 doi: 10.1039/C3NP70054B – ident: e_1_2_2_14_3 doi: 10.1002/(SICI)1521-3757(19980202)110:3<339::AID-ANGE339>3.0.CO;2-F – ident: e_1_2_2_13_2 doi: 10.1021/cr00032a005 – ident: e_1_2_2_34_2 doi: 10.1021/ja505442h – ident: e_1_2_2_12_2 – ident: e_1_2_2_8_2 doi: 10.1021/bi902176v – ident: e_1_2_2_18_2 doi: 10.1016/0584-8539(86)80095-2 – ident: e_1_2_2_27_2 – ident: e_1_2_2_5_2 doi: 10.1021/bi901713r – ident: e_1_2_2_17_2 doi: 10.1016/1010-6030(93)85048-D – ident: e_1_2_2_25_3 doi: 10.1002/ange.201301215 – ident: e_1_2_2_30_2 doi: 10.1126/science.1138249 – ident: e_1_2_2_16_2 doi: 10.1039/P29900000837 – ident: e_1_2_2_31_2 – ident: e_1_2_2_32_2 doi: 10.1016/j.trac.2007.09.003 – ident: e_1_2_2_29_2 doi: 10.1007/s10811-013-0203-4 – ident: e_1_2_2_11_2 doi: 10.1016/j.tibtech.2009.11.002 – ident: e_1_2_2_28_2 doi: 10.1021/cb6003965 – ident: e_1_2_2_14_2 doi: 10.1002/(SICI)1521-3773(19980216)37:3<325::AID-ANIE325>3.0.CO;2-L – ident: e_1_2_2_21_2 doi: 10.1021/ja4042059 – ident: e_1_2_2_22_2 doi: 10.1074/jbc.M305459200 – volume: 250 start-page: 5289 year: 1975 ident: WOS:A1975AK27200002 article-title: MULTIPLE FORMS OF BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHETASE IN ESCHERICHIA-COLI publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY – volume: 29 start-page: 1111 year: 2012 ident: WOS:000308659700006 article-title: The structural role of the carrier protein - active controller or passive carrier publication-title: NATURAL PRODUCT REPORTS doi: 10.1039/c2np20062g – volume: 130 start-page: 13630 year: 2008 ident: WOS:000259924000031 article-title: A versatile amino acid analogue of the solvatochromic fluorophore 4-N,N-dimethylamino-1,8-naphthalimide: A powerful tool for the study of dynamic protein interactions publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja804754y – volume: 28 start-page: 73 year: 2010 ident: WOS:000274556900003 article-title: Monitoring protein interactions and dynamics with solvatochromic fluorophores publication-title: TRENDS IN BIOTECHNOLOGY doi: 10.1016/j.tibtech.2009.11.002 – volume: 136 start-page: 11240 year: 2014 ident: WOS:000340442700009 article-title: Probing the Phosphopantetheine Arm Conformations of Acyl Carrier Proteins Using Vibrational Spectroscopy publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja505442h – volume: 45 start-page: 5217 year: 2006 ident: WOS:000237049400014 article-title: Solution structures of spinach acyl carrier protein with decanoate and stearate publication-title: BIOCHEMISTRY doi: 10.1021/bi052062d – volume: 110 start-page: 339 year: 1998 ident: 000346485800027.15 publication-title: Angew. Chem – volume: 460 start-page: 157 year: 2014 ident: WOS:000336414300002 article-title: The chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal publication-title: BIOCHEMICAL JOURNAL doi: 10.1042/BJ20140239 – volume: 316 start-page: 288 year: 2007 ident: WOS:000245654500054 article-title: Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase publication-title: SCIENCE doi: 10.1126/science.1138249 – volume: 94 start-page: 2319 year: 1994 ident: WOS:A1994PY50400005 article-title: SOLVATOCHROMIC DYES AS SOLVENT POLARITY INDICATORS publication-title: CHEMICAL REVIEWS – volume: 26 start-page: 1619 year: 2014 ident: WOS:000340101100001 article-title: Evolution of acyl-ACP thioesterases and beta-ketoacyl-ACP synthases revealed by protein-protein interactions publication-title: JOURNAL OF APPLIED PHYCOLOGY doi: 10.1007/s10811-013-0203-4 – volume: 26 start-page: 884 year: 2007 ident: WOS:000250846800015 article-title: Exploring biomolecular interactions by single-molecule fluorescence publication-title: TRAC-TRENDS IN ANALYTICAL CHEMISTRY doi: 10.1016/j.trac.2007.09.003 – volume: 37 start-page: 325 year: 1998 ident: WOS:000072138500018 article-title: Synthesis of a new class of solvent-sensitive fluorescent labels publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION – volume: 31 start-page: 61 year: 2014 ident: WOS:000329887500004 article-title: The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life publication-title: NATURAL PRODUCT REPORTS doi: 10.1039/c3np70054b – volume: 4 start-page: 44 year: 2006 ident: WOS:000233968100008 article-title: One-pot chemo-enzymatic synthesis of reporter-modified proteins publication-title: ORGANIC & BIOMOLECULAR CHEMISTRY doi: 10.1039/b512735a – volume: 1 start-page: 687 year: 2006 ident: WOS:000243895300013 article-title: Mechanism-based protein cross-linking probes to investigate carrier protein-mediated biosynthesis publication-title: ACS CHEMICAL BIOLOGY doi: 10.1021/cb6003965 – year: 2014 ident: 000346485800027.23 publication-title: Nobel Prize in Chemistry – volume: 125 start-page: 8909 year: 2013 ident: 000346485800027.20 publication-title: Angew. Chem – volume: 266 start-page: 1858 year: 1991 ident: WOS:A1991EU49700075 article-title: INVIVO POOLS OF FREE AND ACYLATED ACYL CARRIER PROTEINS IN SPINACH - EVIDENCE FOR SITES OF REGULATION OF FATTY-ACID BIOSYNTHESIS publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY – start-page: 837 year: 1990 ident: WOS:A1990DD96000029 article-title: THE UV-VISIBLE ABSORPTION AND FLUORESCENCE OF SOME SUBSTITUTED 1,8-NAPHTHALIMIDES AND NAPHTHALIC ANHYDRIDES publication-title: JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2 – volume: 117 start-page: 15935 year: 2013 ident: WOS:000328920600003 article-title: Two-Photon Fluorescence Spectroscopy and Imaging of 4-Dimethylaminonaphthalimide Peptide and Protein Conjugates publication-title: JOURNAL OF PHYSICAL CHEMISTRY B doi: 10.1021/jp407321g – volume: 278 start-page: 33142 year: 2003 ident: WOS:000184901800080 article-title: Cloning, expression, and characterization of a human 4 '-phosphopantetheinyl transferase with broad substrate specificity publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY doi: 10.1074/jbc.M305459200 – volume: 135 start-page: 8846 year: 2013 ident: WOS:000320899200021 article-title: Sulfonyl 3-Alkynyi Pantetheinamides as Mechanism-Based Cross-Linkers of Acyl Carrier Protein Dehydratase publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja4042059 – volume: 52 start-page: 8746 year: 2013 ident: WOS:000322835700055 article-title: NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION doi: 10.1002/anie.201301215 – volume: 42 start-page: 747 year: 1986 ident: WOS:A1986D018700009 article-title: SOLVATOCHROMISM AND THERMOCHROMISM OF RHODAMINE SOLUTIONS publication-title: SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY – volume: 505 start-page: 427 year: 2014 ident: WOS:000329621800048 article-title: Trapping the dynamic acyl carrier protein in fatty acid biosynthesis publication-title: NATURE doi: 10.1038/nature12810 – volume: 85 start-page: 649 year: 2007 ident: WOS:000252316300001 article-title: Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family publication-title: BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE doi: 10.1139/O07-109 – volume: 505 start-page: 422 year: 2014 ident: WOS:000329621800047 article-title: Chasing acyl carrier protein through a catalytic cycle of lipid A production publication-title: NATURE doi: 10.1038/nature12679 – volume: 283 start-page: 518 year: 2008 ident: WOS:000251940300057 article-title: A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY doi: 10.1074/jbc.M703454200 – volume: 49 start-page: 2186 year: 2010 ident: WOS:000275227000011 article-title: Solution Structure of an Acyl Carrier Protein Domain from a Fungal Type I Polyketide Synthase publication-title: BIOCHEMISTRY doi: 10.1021/bi902176v – volume: 49 start-page: 2860 year: 2010 ident: WOS:000275978900012 article-title: Molecular Dynamics Simulations of beta-Ketoacyl-, beta-Hydroxyacyl-, and trans-2-Enoyl-Acyl Carrier Proteins of Escherichia coli publication-title: BIOCHEMISTRY doi: 10.1021/bi901713r
SSID	ssj0028806
Score	2.3451416
Snippet	The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly... In the fatty acid biosynthesis of plants and bacteria, the acyl carrier protein (ACP) is known to sequester elongating products within its hydrophobic core,...
Source	Web of Science
SourceID	pubmedcentral osti proquest pubmed webofscience crossref wiley istex
SourceType	Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	14456
SubjectTerms	acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - metabolism BASIC BIOLOGICAL SCIENCES Biosynthesis Carriers Catalysis Catalysts chain-flipping mechanism Chains Chemistry Chemistry, Multidisciplinary E coli Elongation Escherichia coli fatty acid synthase Fatty acids Fatty Acids - biosynthesis Fluorescence Naphthalimides - chemistry Nuclear Magnetic Resonance, Biomolecular Oxadiazoles - chemistry Physical Sciences Protein Interaction Domains and Motifs Proteins Rhodamines - chemistry Science & Technology solvatochromism Solvents - chemistry
Title	Visualizing the Chain-Flipping Mechanism in Fatty-Acid Biosynthesis
URI	https://api.istex.fr/ark:/67375/WNG-LMGQ30PL-L/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.201408576 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000346485800027 https://www.ncbi.nlm.nih.gov/pubmed/25354391 https://www.proquest.com/docview/1636824827 https://www.proquest.com/docview/1639494727 https://www.proquest.com/docview/1701002571 https://www.osti.gov/servlets/purl/1342736 https://pubmed.ncbi.nlm.nih.gov/PMC4425425
Volume	53
WOS	000346485800027
WOSCitedRecordID	wos000346485800027
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVWIB databaseName: Wiley Online Library Full Collection 2020 customDbUrl: eissn: 1521-3773 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0028806 issn: 1433-7851 databaseCode: DRFUL dateStart: 19980101 isFulltext: true titleUrlDefault: https://onlinelibrary.wiley.com providerName: Wiley-Blackwell
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwED-xFgle-P4IG1OQJniK1jqO7TyWshakrhqIwd6sxHFYxEhRkyHGE38CfyN_CXdJalZpfAikqkrqs-X6PnxO7n4HsJMpzpG1UZBJIwKueBbETOHXIExzE1ubpnlTbELO5-roKD44l8Xf4kO4B26kGY29JgVP0mr3J2goZWBTaBZBdEmxAX2Gwhv1oP_s1eRw5g5dKJ9thlEYBlSIfgXcOGC76yOsbUx9WuPPaKYXqGgXOZ8Xx1C6fWvd1W32qsn1__-XN-Ba56f6o1awbsIlW96CK-NVebjbMH1TVJSQ-QX3Ph-9SH98nBTl96_fJicN5sM7f99SVnFRffCL0p8kdX2GrSNTZP7TYlGdldipKqo7cDjZez1-HnRVGQIjRCwCFqk8QysQZ6jPRg5yZYVIkbO5yUWaWpmmkVJ40syGCWMms3Smwp-l4HjNbHgXeuWitPfBH6bYMZcxS3jGbW5jEdscR5Y5s4mSzINgxRJtOshyqpxxoluwZaZpebRbHg-eOPqPLVjHLykfNxx2ZMnyPYW4yUi_nU_1bH_6MhwczPTMg00SAY18JVBdQ9FHptbDkKPfh8NsrSRDd7pfafRwhWIEr-rBI9eM3KFXMUlpF6cNTcxjLn9LIwc080gOPbjXCpubLovCiHKmPZBrYugICDV8vaUsjhv0cI5WGj8e7JwXWNexQSwSXEWqeSvtwfBvyMYddwhIofaANSL9Bx7o0fzFnrt78C-dNuEqXVN4EWNb0KuXp_YhXDaf6qJabsOGPFLbnUH4ASMOYNA
linkProvider	Wiley-Blackwell
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwED_BijRe-B6EDQjSBE_RUsexncdS1m6irQbaYG9W4jgsYqSoyRDjiT-Bv5G_hLskDVQaH0JIVdTEZyvxffic3P0OYDtVnCNrQy-VRnhc8dSLmMKDHySZiaxNkqwuNiFnM3V8HB200YSUC9PgQ3Qv3EgzantNCk4vpHd-oIZSCjbFZhFGlxSXocdRllDIe89fjY4m3a4LBbRJMQoCjyrRL5EbfbazOsLKytSjSf6EdnqOmnaR93lxEGW3cK36uvViNbr-Hx7zBlxrPVV30IjWTbhki1uwPlwWiLsN49d5SSmZn3H1c9GPdIcncV58-_J1dFqjPrx1p5byivPyvZsX7iiuqnNsHZg8dZ_l8_K8wE5lXt6Bo9Hu4XDPa-syeEaISHgsVFmKdiBKUaON9DNlhUiQt5nJRJJYmSShUrjXTPsxYya1tKvCy1Jw_M9ssAFrxbyw98DtJ9gxkxGLecptZiMR2QxHlhmzsZLMAW_JE21a0HKqnXGqG7hlpml6dDc9Djzt6D80cB2_pHxSs7gjixfvKMhNhvrNbKwn0_HLwD-Y6IkDmyQDGhlLsLqG4o9MpfsBR88Ph9laioZutb_U6OMKxQhg1YHHXTNyhz7GxIWdn9U0EY-4_C2N9OnOQ9l34G4jbd3tsjAIKWvaAbkihx0B4YavthT5SY0fztFO48-B7Z8ltutYYxYJrkJVf5d2oP83ZMOWOwSlUDnAapn-Aw_0YLa_253d_5dOj2B973CKbNqfvdiEq3Sdgo0Y24K1anFmH8AV87HKy8XD1i58B9iqY9g
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwED9Bi4AXPgeEDQjSBE_RWsexncfSLWWiqwZisDcrHzaLGOnUZIjxxJ_A38hfwl2SBiqNDyGkqmris-X6PnxO7n4HsJkpzpG1gZfJVHhc8cwLmcKvgZ_YNDQmSWxdbELOZurwMNxvowkpF6bBh-geuJFm1PaaFNycZHbrB2oopWBTbBZhdElxEfqcKsn0oL_9KjqYdqcuFNAmxcj3PapEv0RuHLCt1RFWdqY-LfIntNNz1LTzvM_zgyi7jWvV1603q-j6f_ibN-Ba66m6o0a0bsIFU9yCK-NlgbjbMHmTl5SS-Rl3Pxf9SHd8FOfFty9fo-Ma9eGdu2corzgvP7h54UZxVZ1h6yjNM_dZPi_PCuxU5uUaHEQ7r8fPvbYug5cKEQqPBcpmaAfCDDU6lQOrjBAJ8tamViSJkUkSKIVnzWwYM5Zmhk5VeFsKjr-Z8e9Ar5gX5h64wwQ7WhmymGfcWBOK0FgcWVpmYiWZA96SJzptQcupdsaxbuCWmabl0d3yOPC0oz9p4Dp-SfmkZnFHFi_eU5CbDPTb2URP9yYv_cH-VE8dWCcZ0MhYgtVNKf4orfTQ5-j54TAbS9HQrfaXGn1coRgBrDrwuGtG7tDLmLgw89OaJuQhl7-lkQOaeSCHDtxtpK2bLgv8gLKmHZArctgREG74akuRH9X44RztNH4c2PxZYruONWaR4CpQ9XtpB4Z_QzZuuUNQCpUDrJbpP_BAj2a7O93V_X_p9Agu729Hero7e7EOV-k2xRoxtgG9anFqHsCl9GOVl4uHrVn4DtMRY1M
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Visualizing+the+Chain-Flipping+Mechanism+in+Fatty-Acid+Biosynthesis&rft.jtitle=Angewandte+Chemie+International+Edition&rft.au=Beld%2C+Joris&rft.au=Cang%2C+Hu&rft.au=Burkart%2C+Michael+D.&rft.date=2014-12-22&rft.pub=Wiley&rft.issn=1433-7851&rft.eissn=1521-3773&rft.volume=53&rft.issue=52&rft.spage=14456&rft.epage=14461&rft_id=info:doi/10.1002%2Fanie.201408576&rft_id=info%3Apmid%2F25354391&rft.externalDBID=n%2Fa&rft.externalDocID=000346485800027
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1433-7851&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1433-7851&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1433-7851&client=summon