[25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis
This chapter provides an overview of capsular poly-γ-D-glutamate synthesis in Bacillus licheniformis. A membranous polyglutamyl synthetase complex (PGSC) from Bacillus licheniformis 9945A catalyzes a sequence of membrane-associated enzymatic reactions in which L-glutamic acid is activated, racemized...
Gespeichert in:
| Veröffentlicht in: | Methods in Enzymology 1985, Vol.113, p.146-168 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 168 |
|---|---|
| container_issue | |
| container_start_page | 146 |
| container_title | Methods in Enzymology |
| container_volume | 113 |
| creator | Troy, Frederic A. |
| description | This chapter provides an overview of capsular poly-γ-D-glutamate synthesis in Bacillus licheniformis. A membranous polyglutamyl synthetase complex (PGSC) from Bacillus licheniformis 9945A catalyzes a sequence of membrane-associated enzymatic reactions in which L-glutamic acid is activated, racemized, and polymerized to form a poly(γ-D-glutamyl) capsule. The molecular mass of these surface polymers exceeds 106 daltons. The capsule is important in the pathogenicity of Bacillus anthracis because of its ability to influence host–cell interactions. The in vitro determination of the overall reaction catalyzed by the membranous PGSC is based on measuring the rate of incorporation of L-[U-14C]glutamic acid into the high-molecular-weight polymeric products (poly-γ-D-glutamic acid, PGA). These polymers are chromatographically and electrophoretically immobile. The activity of the L-glutamic acid activating enzyme is determined by measuring the rate of an ATP-dependent formation of [14C]glutamyl hydroxamate. |
| doi_str_mv | 10.1016/S0076-6879(85)13028-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_76574678</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0076687985130284</els_id><sourcerecordid>76574678</sourcerecordid><originalsourceid>FETCH-LOGICAL-c314t-cb1538f88f8d0bb77275399f93c0cc448211a6fa69f1bcf07f9fc4c9ccf6ec73</originalsourceid><addsrcrecordid>eNo9kMtOwzAQRS0eKqX0EyplhWBh8COJ7RWCqjykSizoDiHLmdjUyE1KnCD1u_gPvomUVkgjzeLemblzEJpQckUJza9fCBE5zqVQFzK7pJwwidMDNKRZJrBQUh6isRKSUEYlI5TLIzT8HzlBpzF-EMKEVHSABiylknM2RLNXlr0lU7OOXTBNsq7DBv984xK_h641K9PaJG6qdmmjj4mvkjsDPoQuJsHD0lbe1c3KxzN07EyIdrzvI7S4ny2mj3j-_PA0vZ1j4DRtMRQ049LJvkpSFEIwkXGlnOJAANJUMkpN7kyuHC3AEeGUgxQUgMstCD5C57u166b-7GxsdX8bbAimsnUXtcgzkeZC9sbJ3tgVK1vqdeNXptno_du9frPTbR_2y9tGR_C2Alv6xkKry9prSvSWu_7jrrcQtcz0H3ed8l9Hf3Kp</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76574678</pqid></control><display><type>article</type><title>[25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis</title><source>MEDLINE</source><source>ScienceDirect eBooks</source><source>Access via ScienceDirect (Elsevier)</source><creator>Troy, Frederic A.</creator><creatorcontrib>Troy, Frederic A.</creatorcontrib><description>This chapter provides an overview of capsular poly-γ-D-glutamate synthesis in Bacillus licheniformis. A membranous polyglutamyl synthetase complex (PGSC) from Bacillus licheniformis 9945A catalyzes a sequence of membrane-associated enzymatic reactions in which L-glutamic acid is activated, racemized, and polymerized to form a poly(γ-D-glutamyl) capsule. The molecular mass of these surface polymers exceeds 106 daltons. The capsule is important in the pathogenicity of Bacillus anthracis because of its ability to influence host–cell interactions. The in vitro determination of the overall reaction catalyzed by the membranous PGSC is based on measuring the rate of incorporation of L-[U-14C]glutamic acid into the high-molecular-weight polymeric products (poly-γ-D-glutamic acid, PGA). These polymers are chromatographically and electrophoretically immobile. The activity of the L-glutamic acid activating enzyme is determined by measuring the rate of an ATP-dependent formation of [14C]glutamyl hydroxamate.</description><identifier>ISSN: 0076-6879</identifier><identifier>ISBN: 9780121820138</identifier><identifier>ISBN: 0121820130</identifier><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/S0076-6879(85)13028-4</identifier><identifier>PMID: 2418332</identifier><language>eng</language><publisher>United States: Elsevier Science & Technology</publisher><subject>Bacillus - growth & development ; Bacillus - metabolism ; Carbon Radioisotopes ; Cell Membrane - enzymology ; Glutamates - biosynthesis ; Glutamates - isolation & purification ; Glutamates - metabolism ; Kinetics ; Peptide Biosynthesis ; Peptide Synthases - metabolism ; Peptides - isolation & purification ; Polyglutamic Acid - biosynthesis ; Polyglutamic Acid - isolation & purification ; Polyglutamic Acid - metabolism ; Radioisotope Dilution Technique</subject><ispartof>Methods in Enzymology, 1985, Vol.113, p.146-168</ispartof><rights>1985</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c314t-cb1538f88f8d0bb77275399f93c0cc448211a6fa69f1bcf07f9fc4c9ccf6ec73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0076687985130284$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,780,781,785,794,3460,3551,4025,11293,27928,27929,27930,45815,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2418332$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Troy, Frederic A.</creatorcontrib><title>[25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis</title><title>Methods in Enzymology</title><addtitle>Methods Enzymol</addtitle><description>This chapter provides an overview of capsular poly-γ-D-glutamate synthesis in Bacillus licheniformis. A membranous polyglutamyl synthetase complex (PGSC) from Bacillus licheniformis 9945A catalyzes a sequence of membrane-associated enzymatic reactions in which L-glutamic acid is activated, racemized, and polymerized to form a poly(γ-D-glutamyl) capsule. The molecular mass of these surface polymers exceeds 106 daltons. The capsule is important in the pathogenicity of Bacillus anthracis because of its ability to influence host–cell interactions. The in vitro determination of the overall reaction catalyzed by the membranous PGSC is based on measuring the rate of incorporation of L-[U-14C]glutamic acid into the high-molecular-weight polymeric products (poly-γ-D-glutamic acid, PGA). These polymers are chromatographically and electrophoretically immobile. The activity of the L-glutamic acid activating enzyme is determined by measuring the rate of an ATP-dependent formation of [14C]glutamyl hydroxamate.</description><subject>Bacillus - growth & development</subject><subject>Bacillus - metabolism</subject><subject>Carbon Radioisotopes</subject><subject>Cell Membrane - enzymology</subject><subject>Glutamates - biosynthesis</subject><subject>Glutamates - isolation & purification</subject><subject>Glutamates - metabolism</subject><subject>Kinetics</subject><subject>Peptide Biosynthesis</subject><subject>Peptide Synthases - metabolism</subject><subject>Peptides - isolation & purification</subject><subject>Polyglutamic Acid - biosynthesis</subject><subject>Polyglutamic Acid - isolation & purification</subject><subject>Polyglutamic Acid - metabolism</subject><subject>Radioisotope Dilution Technique</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>9780121820138</isbn><isbn>0121820130</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtOwzAQRS0eKqX0EyplhWBh8COJ7RWCqjykSizoDiHLmdjUyE1KnCD1u_gPvomUVkgjzeLemblzEJpQckUJza9fCBE5zqVQFzK7pJwwidMDNKRZJrBQUh6isRKSUEYlI5TLIzT8HzlBpzF-EMKEVHSABiylknM2RLNXlr0lU7OOXTBNsq7DBv984xK_h641K9PaJG6qdmmjj4mvkjsDPoQuJsHD0lbe1c3KxzN07EyIdrzvI7S4ny2mj3j-_PA0vZ1j4DRtMRQ049LJvkpSFEIwkXGlnOJAANJUMkpN7kyuHC3AEeGUgxQUgMstCD5C57u166b-7GxsdX8bbAimsnUXtcgzkeZC9sbJ3tgVK1vqdeNXptno_du9frPTbR_2y9tGR_C2Alv6xkKry9prSvSWu_7jrrcQtcz0H3ed8l9Hf3Kp</recordid><startdate>1985</startdate><enddate>1985</enddate><creator>Troy, Frederic A.</creator><general>Elsevier Science & Technology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1985</creationdate><title>[25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis</title><author>Troy, Frederic A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c314t-cb1538f88f8d0bb77275399f93c0cc448211a6fa69f1bcf07f9fc4c9ccf6ec73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Bacillus - growth & development</topic><topic>Bacillus - metabolism</topic><topic>Carbon Radioisotopes</topic><topic>Cell Membrane - enzymology</topic><topic>Glutamates - biosynthesis</topic><topic>Glutamates - isolation & purification</topic><topic>Glutamates - metabolism</topic><topic>Kinetics</topic><topic>Peptide Biosynthesis</topic><topic>Peptide Synthases - metabolism</topic><topic>Peptides - isolation & purification</topic><topic>Polyglutamic Acid - biosynthesis</topic><topic>Polyglutamic Acid - isolation & purification</topic><topic>Polyglutamic Acid - metabolism</topic><topic>Radioisotope Dilution Technique</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Troy, Frederic A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Troy, Frederic A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>[25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>1985</date><risdate>1985</risdate><volume>113</volume><spage>146</spage><epage>168</epage><pages>146-168</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>9780121820138</isbn><isbn>0121820130</isbn><abstract>This chapter provides an overview of capsular poly-γ-D-glutamate synthesis in Bacillus licheniformis. A membranous polyglutamyl synthetase complex (PGSC) from Bacillus licheniformis 9945A catalyzes a sequence of membrane-associated enzymatic reactions in which L-glutamic acid is activated, racemized, and polymerized to form a poly(γ-D-glutamyl) capsule. The molecular mass of these surface polymers exceeds 106 daltons. The capsule is important in the pathogenicity of Bacillus anthracis because of its ability to influence host–cell interactions. The in vitro determination of the overall reaction catalyzed by the membranous PGSC is based on measuring the rate of incorporation of L-[U-14C]glutamic acid into the high-molecular-weight polymeric products (poly-γ-D-glutamic acid, PGA). These polymers are chromatographically and electrophoretically immobile. The activity of the L-glutamic acid activating enzyme is determined by measuring the rate of an ATP-dependent formation of [14C]glutamyl hydroxamate.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>2418332</pmid><doi>10.1016/S0076-6879(85)13028-4</doi><tpages>23</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0076-6879 |
| ispartof | Methods in Enzymology, 1985, Vol.113, p.146-168 |
| issn | 0076-6879 1557-7988 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76574678 |
| source | MEDLINE; ScienceDirect eBooks; Access via ScienceDirect (Elsevier) |
| subjects | Bacillus - growth & development Bacillus - metabolism Carbon Radioisotopes Cell Membrane - enzymology Glutamates - biosynthesis Glutamates - isolation & purification Glutamates - metabolism Kinetics Peptide Biosynthesis Peptide Synthases - metabolism Peptides - isolation & purification Polyglutamic Acid - biosynthesis Polyglutamic Acid - isolation & purification Polyglutamic Acid - metabolism Radioisotope Dilution Technique |
| title | [25] Capsular poly-γ-d-glutamate synthesis in Bacillus licheniformis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-15T01%3A39%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=%5B25%5D%20Capsular%20poly-%CE%B3-d-glutamate%20synthesis%20in%20Bacillus%20licheniformis&rft.jtitle=Methods%20in%20Enzymology&rft.au=Troy,%20Frederic%20A.&rft.date=1985&rft.volume=113&rft.spage=146&rft.epage=168&rft.pages=146-168&rft.issn=0076-6879&rft.eissn=1557-7988&rft.isbn=9780121820138&rft.isbn_list=0121820130&rft_id=info:doi/10.1016/S0076-6879(85)13028-4&rft_dat=%3Cproquest_pubme%3E76574678%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76574678&rft_id=info:pmid/2418332&rft_els_id=S0076687985130284&rfr_iscdi=true |