Lipolytic enzymes in Mycobacterium tuberculosis
Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose...
Gespeichert in:
Veröffentlicht in: | Applied microbiology and biotechnology 2008-04, Vol.78 (5), p.741-749 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 749 |
---|---|
container_issue | 5 |
container_start_page | 741 |
container_title | Applied microbiology and biotechnology |
container_volume | 78 |
creator | Côtes, K Bakala N'Goma, J. C Dhouib, R Douchet, I Maurin, D Carrière, F Canaan, S |
description | Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose tissues. Indeed, before entering in the dormant state, bacteria accumulate lipids originating from the host cell membrane degradation and from de novo synthesis. During the reactivation phase, these lipids are hydrolysed and the infection process occurs. The degradation of both extra and intracellular lipids can be directly related to the presence of lipolytic enzymes in mycobacteria, which have been ignored during a long period particularly due to the difficulties to obtain a high expression level of these enzymes in M. tuberculosis. The completion of the M. tuberculosis genome offered new opportunity to this kind of study. The aim of this review is to focus on the recent results obtained in the field of mycobacterium lipolytic enzymes and although no experimental proof has been shown in vivo, it is tempting to speculate that these enzymes could be involved in the virulence and pathogenicity processes. |
doi_str_mv | 10.1007/s00253-008-1397-2 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68093418</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1896316121</sourcerecordid><originalsourceid>FETCH-LOGICAL-c497t-edf002941e9872f86eaf608896f133bb2fdcc1dbc9087d9e0144979c6343055f3</originalsourceid><addsrcrecordid>eNqFkMtu2zAQRYmiQeO4_YBuWiNAslM8Q0p8LIMgjwIOski8JiiKNGTo4ZLSwvn60JBRA120Ky547p2ZQ8h3hBsEEMsIQAuWAcgMmRIZ_URmmDOaAcf8M5kBiiIThZLn5CLGLQBSyfkXco6SgcqFnJHlqt71zX6o7cJ17_vWxUXdLZ73ti-NHVyox3YxjKULdmz6WMev5MybJrpvx3dO1g_3b3dP2erl8dfd7SqzuRJD5iqfdlM5OiUF9ZI74zlIqbhHxsqS-sparEqrQIpKOcA85ZTlLGdQFJ7NyfXUuwv979HFQbd1tK5pTOf6MWouQbE83fE_kCaOoWAJvPwL3PZj6NIRmlLFgSIc2nCCbOhjDM7rXahbE_YaQR-c68m5Ts71wbmmKfPjWDyWratOiaPkBFwdAROtaXwwna3jH46m0aKQReLoxMX01W1cOG34r-k_p5A3vTabkIrXrxSQJUYUAoB9ACmboDY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>229602108</pqid></control><display><type>article</type><title>Lipolytic enzymes in Mycobacterium tuberculosis</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Côtes, K ; Bakala N'Goma, J. C ; Dhouib, R ; Douchet, I ; Maurin, D ; Carrière, F ; Canaan, S</creator><creatorcontrib>Côtes, K ; Bakala N'Goma, J. C ; Dhouib, R ; Douchet, I ; Maurin, D ; Carrière, F ; Canaan, S</creatorcontrib><description>Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose tissues. Indeed, before entering in the dormant state, bacteria accumulate lipids originating from the host cell membrane degradation and from de novo synthesis. During the reactivation phase, these lipids are hydrolysed and the infection process occurs. The degradation of both extra and intracellular lipids can be directly related to the presence of lipolytic enzymes in mycobacteria, which have been ignored during a long period particularly due to the difficulties to obtain a high expression level of these enzymes in M. tuberculosis. The completion of the M. tuberculosis genome offered new opportunity to this kind of study. The aim of this review is to focus on the recent results obtained in the field of mycobacterium lipolytic enzymes and although no experimental proof has been shown in vivo, it is tempting to speculate that these enzymes could be involved in the virulence and pathogenicity processes.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-008-1397-2</identifier><identifier>PMID: 18309478</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Adipocytes ; Adipose tissue ; Amino Acid Sequence ; Bacillus ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological and medical sciences ; Biotechnology ; Carbon ; Drug resistance ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Genomes ; granuloma ; Granulomas ; Humans ; Immune system ; infection ; Infections ; Infectious diseases ; Life Sciences ; Lipase - chemistry ; Lipase - genetics ; Lipase - metabolism ; Lipid Metabolism ; Lipidic inclusion bodies ; Lipids ; Metabolism ; Microbial Genetics and Genomics ; Microbiology ; Mini-Review ; Molecular Sequence Data ; Mycobacterium - enzymology ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - enzymology ; Mycobacterium tuberculosis - genetics ; Mycobacterium tuberculosis - metabolism ; Pathogens ; Phospholipase ; Phospholipases - chemistry ; Phospholipases - genetics ; Phospholipases - metabolism ; Proteins ; Sequence Alignment ; Studies ; TAG ; triacylglycerol lipase ; Tuberculosis ; Tuberculosis - enzymology ; Tuberculosis - microbiology ; Virulence</subject><ispartof>Applied microbiology and biotechnology, 2008-04, Vol.78 (5), p.741-749</ispartof><rights>Springer-Verlag 2008</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-edf002941e9872f86eaf608896f133bb2fdcc1dbc9087d9e0144979c6343055f3</citedby><cites>FETCH-LOGICAL-c497t-edf002941e9872f86eaf608896f133bb2fdcc1dbc9087d9e0144979c6343055f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-008-1397-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-008-1397-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20217585$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18309478$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Côtes, K</creatorcontrib><creatorcontrib>Bakala N'Goma, J. C</creatorcontrib><creatorcontrib>Dhouib, R</creatorcontrib><creatorcontrib>Douchet, I</creatorcontrib><creatorcontrib>Maurin, D</creatorcontrib><creatorcontrib>Carrière, F</creatorcontrib><creatorcontrib>Canaan, S</creatorcontrib><title>Lipolytic enzymes in Mycobacterium tuberculosis</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose tissues. Indeed, before entering in the dormant state, bacteria accumulate lipids originating from the host cell membrane degradation and from de novo synthesis. During the reactivation phase, these lipids are hydrolysed and the infection process occurs. The degradation of both extra and intracellular lipids can be directly related to the presence of lipolytic enzymes in mycobacteria, which have been ignored during a long period particularly due to the difficulties to obtain a high expression level of these enzymes in M. tuberculosis. The completion of the M. tuberculosis genome offered new opportunity to this kind of study. The aim of this review is to focus on the recent results obtained in the field of mycobacterium lipolytic enzymes and although no experimental proof has been shown in vivo, it is tempting to speculate that these enzymes could be involved in the virulence and pathogenicity processes.</description><subject>Adipocytes</subject><subject>Adipose tissue</subject><subject>Amino Acid Sequence</subject><subject>Bacillus</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carbon</subject><subject>Drug resistance</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genomes</subject><subject>granuloma</subject><subject>Granulomas</subject><subject>Humans</subject><subject>Immune system</subject><subject>infection</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Life Sciences</subject><subject>Lipase - chemistry</subject><subject>Lipase - genetics</subject><subject>Lipase - metabolism</subject><subject>Lipid Metabolism</subject><subject>Lipidic inclusion bodies</subject><subject>Lipids</subject><subject>Metabolism</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mini-Review</subject><subject>Molecular Sequence Data</subject><subject>Mycobacterium - enzymology</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - enzymology</subject><subject>Mycobacterium tuberculosis - genetics</subject><subject>Mycobacterium tuberculosis - metabolism</subject><subject>Pathogens</subject><subject>Phospholipase</subject><subject>Phospholipases - chemistry</subject><subject>Phospholipases - genetics</subject><subject>Phospholipases - metabolism</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Studies</subject><subject>TAG</subject><subject>triacylglycerol lipase</subject><subject>Tuberculosis</subject><subject>Tuberculosis - enzymology</subject><subject>Tuberculosis - microbiology</subject><subject>Virulence</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkMtu2zAQRYmiQeO4_YBuWiNAslM8Q0p8LIMgjwIOski8JiiKNGTo4ZLSwvn60JBRA120Ky547p2ZQ8h3hBsEEMsIQAuWAcgMmRIZ_URmmDOaAcf8M5kBiiIThZLn5CLGLQBSyfkXco6SgcqFnJHlqt71zX6o7cJ17_vWxUXdLZ73ti-NHVyox3YxjKULdmz6WMev5MybJrpvx3dO1g_3b3dP2erl8dfd7SqzuRJD5iqfdlM5OiUF9ZI74zlIqbhHxsqS-sparEqrQIpKOcA85ZTlLGdQFJ7NyfXUuwv979HFQbd1tK5pTOf6MWouQbE83fE_kCaOoWAJvPwL3PZj6NIRmlLFgSIc2nCCbOhjDM7rXahbE_YaQR-c68m5Ts71wbmmKfPjWDyWratOiaPkBFwdAROtaXwwna3jH46m0aKQReLoxMX01W1cOG34r-k_p5A3vTabkIrXrxSQJUYUAoB9ACmboDY</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Côtes, K</creator><creator>Bakala N'Goma, J. C</creator><creator>Dhouib, R</creator><creator>Douchet, I</creator><creator>Maurin, D</creator><creator>Carrière, F</creator><creator>Canaan, S</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>20080401</creationdate><title>Lipolytic enzymes in Mycobacterium tuberculosis</title><author>Côtes, K ; Bakala N'Goma, J. C ; Dhouib, R ; Douchet, I ; Maurin, D ; Carrière, F ; Canaan, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-edf002941e9872f86eaf608896f133bb2fdcc1dbc9087d9e0144979c6343055f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adipocytes</topic><topic>Adipose tissue</topic><topic>Amino Acid Sequence</topic><topic>Bacillus</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carbon</topic><topic>Drug resistance</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genomes</topic><topic>granuloma</topic><topic>Granulomas</topic><topic>Humans</topic><topic>Immune system</topic><topic>infection</topic><topic>Infections</topic><topic>Infectious diseases</topic><topic>Life Sciences</topic><topic>Lipase - chemistry</topic><topic>Lipase - genetics</topic><topic>Lipase - metabolism</topic><topic>Lipid Metabolism</topic><topic>Lipidic inclusion bodies</topic><topic>Lipids</topic><topic>Metabolism</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mini-Review</topic><topic>Molecular Sequence Data</topic><topic>Mycobacterium - enzymology</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - enzymology</topic><topic>Mycobacterium tuberculosis - genetics</topic><topic>Mycobacterium tuberculosis - metabolism</topic><topic>Pathogens</topic><topic>Phospholipase</topic><topic>Phospholipases - chemistry</topic><topic>Phospholipases - genetics</topic><topic>Phospholipases - metabolism</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Studies</topic><topic>TAG</topic><topic>triacylglycerol lipase</topic><topic>Tuberculosis</topic><topic>Tuberculosis - enzymology</topic><topic>Tuberculosis - microbiology</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Côtes, K</creatorcontrib><creatorcontrib>Bakala N'Goma, J. C</creatorcontrib><creatorcontrib>Dhouib, R</creatorcontrib><creatorcontrib>Douchet, I</creatorcontrib><creatorcontrib>Maurin, D</creatorcontrib><creatorcontrib>Carrière, F</creatorcontrib><creatorcontrib>Canaan, S</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>Biological Sciences</collection><collection>ABI/INFORM global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>One Business (ProQuest)</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Côtes, K</au><au>Bakala N'Goma, J. C</au><au>Dhouib, R</au><au>Douchet, I</au><au>Maurin, D</au><au>Carrière, F</au><au>Canaan, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lipolytic enzymes in Mycobacterium tuberculosis</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>78</volume><issue>5</issue><spage>741</spage><epage>749</epage><pages>741-749</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose tissues. Indeed, before entering in the dormant state, bacteria accumulate lipids originating from the host cell membrane degradation and from de novo synthesis. During the reactivation phase, these lipids are hydrolysed and the infection process occurs. The degradation of both extra and intracellular lipids can be directly related to the presence of lipolytic enzymes in mycobacteria, which have been ignored during a long period particularly due to the difficulties to obtain a high expression level of these enzymes in M. tuberculosis. The completion of the M. tuberculosis genome offered new opportunity to this kind of study. The aim of this review is to focus on the recent results obtained in the field of mycobacterium lipolytic enzymes and although no experimental proof has been shown in vivo, it is tempting to speculate that these enzymes could be involved in the virulence and pathogenicity processes.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18309478</pmid><doi>10.1007/s00253-008-1397-2</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0175-7598 |
ispartof | Applied microbiology and biotechnology, 2008-04, Vol.78 (5), p.741-749 |
issn | 0175-7598 1432-0614 |
language | eng |
recordid | cdi_proquest_miscellaneous_68093418 |
source | MEDLINE; Springer Nature - Complete Springer Journals |
subjects | Adipocytes Adipose tissue Amino Acid Sequence Bacillus Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences Biotechnology Carbon Drug resistance Enzymes Fundamental and applied biological sciences. Psychology Genomes granuloma Granulomas Humans Immune system infection Infections Infectious diseases Life Sciences Lipase - chemistry Lipase - genetics Lipase - metabolism Lipid Metabolism Lipidic inclusion bodies Lipids Metabolism Microbial Genetics and Genomics Microbiology Mini-Review Molecular Sequence Data Mycobacterium - enzymology Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology Mycobacterium tuberculosis - genetics Mycobacterium tuberculosis - metabolism Pathogens Phospholipase Phospholipases - chemistry Phospholipases - genetics Phospholipases - metabolism Proteins Sequence Alignment Studies TAG triacylglycerol lipase Tuberculosis Tuberculosis - enzymology Tuberculosis - microbiology Virulence |
title | Lipolytic enzymes in Mycobacterium tuberculosis |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T17%3A51%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Lipolytic%20enzymes%20in%20Mycobacterium%20tuberculosis&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=C%C3%B4tes,%20K&rft.date=2008-04-01&rft.volume=78&rft.issue=5&rft.spage=741&rft.epage=749&rft.pages=741-749&rft.issn=0175-7598&rft.eissn=1432-0614&rft.coden=AMBIDG&rft_id=info:doi/10.1007/s00253-008-1397-2&rft_dat=%3Cproquest_cross%3E1896316121%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=229602108&rft_id=info:pmid/18309478&rfr_iscdi=true |