The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction
Counting backwards: The cyanobactin class of heterocyclases, exemplified by TruD, possess an almost unique combination of processivity, specificity, chemical versatility, and promiscuity. TruD is shown by biochemical assay to be an adenylase, and processes cysteines in a defined order. The entire su...
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Veröffentlicht in: | Angewandte Chemie International Edition 2013-12, Vol.52 (52), p.13991-13996 |
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creator | Koehnke, Jesko Bent, Andrew F. Zollman, David Smith, Kieran Houssen, Wael E. Zhu, Xiaofeng Mann, Greg Lebl, Tomas Scharff, Richard Shirran, Sally Botting, Catherine H. Jaspars, Marcel Schwarz-Linek, Ulrich Naismith, James H. |
description | Counting backwards: The cyanobactin class of heterocyclases, exemplified by TruD, possess an almost unique combination of processivity, specificity, chemical versatility, and promiscuity. TruD is shown by biochemical assay to be an adenylase, and processes cysteines in a defined order. The entire substrate leader can be removed and TruD will process a single specific cysteine residue; however the role of leader is to permit processivity through a balance of recognition. ATP/AMP=adenosine tri/monophosphate; PPi=pyrophosphate. |
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Chem. Int. Ed</addtitle><description>Counting backwards: The cyanobactin class of heterocyclases, exemplified by TruD, possess an almost unique combination of processivity, specificity, chemical versatility, and promiscuity. TruD is shown by biochemical assay to be an adenylase, and processes cysteines in a defined order. The entire substrate leader can be removed and TruD will process a single specific cysteine residue; however the role of leader is to permit processivity through a balance of recognition. ATP/AMP=adenosine tri/monophosphate; PPi=pyrophosphate.</description><subject>Adenylation</subject><subject>Adenylyl Cyclases - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Balancing</subject><subject>Biochemistry</subject><subject>Counting</subject><subject>Cyanobacteria - genetics</subject><subject>cyanobactins</subject><subject>Cysteine</subject><subject>Enzymes</subject><subject>heterocyclase</subject><subject>Recognition</subject><subject>Residues</subject><subject>ribosomal peptide pathways</subject><subject>Versatility</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFkc9v0zAUxy0EYqNw5YgsceGS4h9xbHNAqkrpJlUroCIkLpaTvFBvqdPZ6Ub463HpqAaXnWz5fd5X7_mD0EtKxpQQ9tZ6B2NGKCcFJ-wROqWC0YxLyR-ne855JpWgJ-hZjJeJV4oUT9EJyxnNCZWn6Gq1BjwdrO9KW_XO4zPoIXTVULU2Ap75X8MG3uEJ_pQeIUZ3A3hSgx_-lFdr2-PlFoLtIeJb16-xxR-gcR5qvAw1BNw1-Avsozv_HD1pbBvhxd05Ql8_zlbTs2yxnJ9PJ4usErJgmeCq1kqVjJdSsRxqRri2pSJVpWpbMFZIUReqbCiXpGwaqWSetq9oKSkXBfARen_I3e7KDdQV-D7Y1myD29gwmM4682_Fu7X50d0YrrUglKWAN3cBobveQezNxsUK2tZ66HbRUElowgQTD6O5JskASUJG6PV_6GW3Cz79RKIKpZMsrRM1PlBV6GIM0BznpsTslZu9cnNUnhpe3d_2iP91nAB9AG5dC8MDcWZycT67H54del3s4eex14YrU0guhfl2MTd8IT5L_V2YOf8N5cvGMg</recordid><startdate>20131223</startdate><enddate>20131223</enddate><creator>Koehnke, Jesko</creator><creator>Bent, Andrew F.</creator><creator>Zollman, David</creator><creator>Smith, Kieran</creator><creator>Houssen, Wael E.</creator><creator>Zhu, Xiaofeng</creator><creator>Mann, Greg</creator><creator>Lebl, Tomas</creator><creator>Scharff, Richard</creator><creator>Shirran, Sally</creator><creator>Botting, Catherine H.</creator><creator>Jaspars, Marcel</creator><creator>Schwarz-Linek, Ulrich</creator><creator>Naismith, James H.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><general>Wiley-VCH Verlag GmbH & Co</general><scope>BSCLL</scope><scope>24P</scope><scope>WIN</scope><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>7TM</scope><scope>K9.</scope><scope>7X8</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>5PM</scope></search><sort><creationdate>20131223</creationdate><title>The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction</title><author>Koehnke, Jesko ; Bent, Andrew F. ; Zollman, David ; Smith, Kieran ; Houssen, Wael E. ; Zhu, Xiaofeng ; Mann, Greg ; Lebl, Tomas ; Scharff, Richard ; Shirran, Sally ; Botting, Catherine H. ; Jaspars, Marcel ; Schwarz-Linek, Ulrich ; Naismith, James H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5762-538d988b23b7824ed2039ab80cc8da622675d68bf1370bff7874063c1b71356e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adenylation</topic><topic>Adenylyl Cyclases - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Balancing</topic><topic>Biochemistry</topic><topic>Counting</topic><topic>Cyanobacteria - genetics</topic><topic>cyanobactins</topic><topic>Cysteine</topic><topic>Enzymes</topic><topic>heterocyclase</topic><topic>Recognition</topic><topic>Residues</topic><topic>ribosomal peptide pathways</topic><topic>Versatility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koehnke, Jesko</creatorcontrib><creatorcontrib>Bent, Andrew F.</creatorcontrib><creatorcontrib>Zollman, David</creatorcontrib><creatorcontrib>Smith, Kieran</creatorcontrib><creatorcontrib>Houssen, Wael E.</creatorcontrib><creatorcontrib>Zhu, Xiaofeng</creatorcontrib><creatorcontrib>Mann, Greg</creatorcontrib><creatorcontrib>Lebl, Tomas</creatorcontrib><creatorcontrib>Scharff, Richard</creatorcontrib><creatorcontrib>Shirran, Sally</creatorcontrib><creatorcontrib>Botting, Catherine H.</creatorcontrib><creatorcontrib>Jaspars, Marcel</creatorcontrib><creatorcontrib>Schwarz-Linek, Ulrich</creatorcontrib><creatorcontrib>Naismith, James H.</creatorcontrib><collection>Istex</collection><collection>Wiley Online Library Open Access</collection><collection>Wiley Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koehnke, Jesko</au><au>Bent, Andrew F.</au><au>Zollman, David</au><au>Smith, Kieran</au><au>Houssen, Wael E.</au><au>Zhu, Xiaofeng</au><au>Mann, Greg</au><au>Lebl, Tomas</au><au>Scharff, Richard</au><au>Shirran, Sally</au><au>Botting, Catherine H.</au><au>Jaspars, Marcel</au><au>Schwarz-Linek, Ulrich</au><au>Naismith, James H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew. 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subjects | Adenylation Adenylyl Cyclases - metabolism Bacterial Proteins - genetics Balancing Biochemistry Counting Cyanobacteria - genetics cyanobactins Cysteine Enzymes heterocyclase Recognition Residues ribosomal peptide pathways Versatility |
title | The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction |
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