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Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia
The peptide amidase (Pam) from the gram-negative bacterium Stenotrophomonas maltophilia catalyzes predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Its gene (pam) was isolated by Southern hybridization using a DNA probe derived from the known terminal amino acid sequence....
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| Published in: | Applied microbiology and biotechnology 2002-05, Vol.58 (6), p.772-780 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Neumann, S Kula, M.R |
| description | The peptide amidase (Pam) from the gram-negative bacterium Stenotrophomonas maltophilia catalyzes predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Its gene (pam) was isolated by Southern hybridization using a DNA probe derived from the known terminal amino acid sequence. Pam is a member of the amidase signature family and was identified as a periplasmic protein by an N-terminal signal peptide found in the gene. The processed protein consists of 503 amino acids with a molecular mass of 53.5 kDa. The recombinant enzyme with a C-terminal His6 tag has a monomeric structure and its isoelectric point is 6.3. The dipeptide amide L-Ala-L-Phe-NH2 is hydrolyzed in the absence of cofactors to L-Ala-L-Phe-OH and ammonia with V(max)=194 U/mg and K(m) |
| doi_str_mv | 10.1007/s00253-002-0943-6 |
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Its gene (pam) was isolated by Southern hybridization using a DNA probe derived from the known terminal amino acid sequence. Pam is a member of the amidase signature family and was identified as a periplasmic protein by an N-terminal signal peptide found in the gene. The processed protein consists of 503 amino acids with a molecular mass of 53.5 kDa. The recombinant enzyme with a C-terminal His6 tag has a monomeric structure and its isoelectric point is 6.3. The dipeptide amide L-Ala-L-Phe-NH2 is hydrolyzed in the absence of cofactors to L-Ala-L-Phe-OH and ammonia with V(max)=194 U/mg and K(m) <0.5 mM. The natural function of Pam remains unclear. Chymostatin (K(i)<0.3 micromolar) and Pefabloc SC (K(i) not determined) were identified as inhibitors. When the gene was expressed in Escherichia coli on a 12-l scale, the specific activity in the crude extract was 60 U/mg, compared to 0.24 U/mg in S. maltophilia. In the expression system, Pam made up about 31% of the total soluble cell protein. From 75 g wet cells, 2.1 g of >95% pure enzyme was obtained, which corresponds to a total activity of 416,000 units.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-002-0943-6</identifier><identifier>PMID: 12021798</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>amidase ; Amides ; Amidohydrolases - chemistry ; Amidohydrolases - genetics ; Amidohydrolases - isolation & purification ; Amidohydrolases - metabolism ; Amino Acid Sequence ; Amino acids ; ammonia ; Bacteria ; Base Sequence ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Chromatography, Gel ; Cloning ; Cloning, Molecular ; DNA ; DNA Probes ; E coli ; Electrophoresis, Polyacrylamide Gel ; Enzyme Inhibitors - pharmacology ; Enzymes ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; gene overexpression ; genes ; Gram-negative bacteria ; hydrolysis ; isoelectric point ; Miscellaneous ; Mission oriented research ; molecular cloning ; Molecular Sequence Data ; molecular weight ; Peptides ; Proteins ; Sequence Homology, Amino Acid ; signal peptide ; Southern blotting ; Stenotrophomonas maltophilia ; Stenotrophomonas maltophilia - enzymology ; Stenotrophomonas maltophilia - genetics ; Substrate Specificity</subject><ispartof>Applied microbiology and biotechnology, 2002-05, Vol.58 (6), p.772-780</ispartof><rights>2002 INIST-CNRS</rights><rights>Springer-Verlag 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c512t-1d9a4fd317668fd82a75f568e8daef9e4c2ce7e1608751813ce73631abeec4013</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/884646897/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/884646897?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,11688,27924,27925,36060,36061,44363,74895</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13654653$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12021798$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Neumann, S</creatorcontrib><creatorcontrib>Kula, M.R</creatorcontrib><title>Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>The peptide amidase (Pam) from the gram-negative bacterium Stenotrophomonas maltophilia catalyzes predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Its gene (pam) was isolated by Southern hybridization using a DNA probe derived from the known terminal amino acid sequence. Pam is a member of the amidase signature family and was identified as a periplasmic protein by an N-terminal signal peptide found in the gene. The processed protein consists of 503 amino acids with a molecular mass of 53.5 kDa. The recombinant enzyme with a C-terminal His6 tag has a monomeric structure and its isoelectric point is 6.3. The dipeptide amide L-Ala-L-Phe-NH2 is hydrolyzed in the absence of cofactors to L-Ala-L-Phe-OH and ammonia with V(max)=194 U/mg and K(m) <0.5 mM. The natural function of Pam remains unclear. Chymostatin (K(i)<0.3 micromolar) and Pefabloc SC (K(i) not determined) were identified as inhibitors. When the gene was expressed in Escherichia coli on a 12-l scale, the specific activity in the crude extract was 60 U/mg, compared to 0.24 U/mg in S. maltophilia. In the expression system, Pam made up about 31% of the total soluble cell protein. From 75 g wet cells, 2.1 g of >95% pure enzyme was obtained, which corresponds to a total activity of 416,000 units.</description><subject>amidase</subject><subject>Amides</subject><subject>Amidohydrolases - chemistry</subject><subject>Amidohydrolases - genetics</subject><subject>Amidohydrolases - isolation & purification</subject><subject>Amidohydrolases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>ammonia</subject><subject>Bacteria</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Chromatography, Gel</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>DNA Probes</subject><subject>E coli</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene overexpression</subject><subject>genes</subject><subject>Gram-negative bacteria</subject><subject>hydrolysis</subject><subject>isoelectric point</subject><subject>Miscellaneous</subject><subject>Mission oriented research</subject><subject>molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>molecular weight</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>signal peptide</subject><subject>Southern blotting</subject><subject>Stenotrophomonas maltophilia</subject><subject>Stenotrophomonas maltophilia - enzymology</subject><subject>Stenotrophomonas maltophilia - genetics</subject><subject>Substrate Specificity</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>M0C</sourceid><recordid>eNqF0U2LFDEQBuAgijuu_gAvGgQ92Zp0Pvsoi67Cgod1z6EmXdnJ0p20Sc-i_nozzMCCFy8VCp4qSL2EvOTsA2fMfKyM9Up0rXZskKLTj8iGS9E6zeVjsmHcqM6owZ6RZ7XeMcZ7q_VTcsZ71nMz2A25v8SE1E85xXT7nuZ7LPhrKVhrzIlCGuk2Zr_DOXqYqN9BAb9iiX9gPYAc6LpDuuCyxhEpzHGEijSUPNPrFVNeS152ec4JKp1hWlsXpwjPyZMAU8UXp_ec3Hz5_OPia3f1_fLbxaerziverx0fB5BhFNxobcNoezAqKG3RjoBhQOl7jwa5ZtYobrlondCCwxbRS8bFOXl33LuU_HOPdXVzrB6nCRLmfXWGGyF783_IrWRMG9vgm3_gXd6X1D7hrJVaajuYhvgR-ZJrLRjcUuIM5bfjzB2ic8foXKvuEJ3TbebVafF-O-P4MHHKqoG3JwC1hREKJB_rgxNaSa1Ec6-PLkB2cFuaubnuWTsSY4NRRoi_rcasEA</recordid><startdate>20020501</startdate><enddate>20020501</enddate><creator>Neumann, S</creator><creator>Kula, M.R</creator><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>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>20020501</creationdate><title>Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia</title><author>Neumann, S ; Kula, M.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c512t-1d9a4fd317668fd82a75f568e8daef9e4c2ce7e1608751813ce73631abeec4013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>amidase</topic><topic>Amides</topic><topic>Amidohydrolases - chemistry</topic><topic>Amidohydrolases - genetics</topic><topic>Amidohydrolases - isolation & purification</topic><topic>Amidohydrolases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>ammonia</topic><topic>Bacteria</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Chromatography, Gel</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>DNA Probes</topic><topic>E coli</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene overexpression</topic><topic>genes</topic><topic>Gram-negative bacteria</topic><topic>hydrolysis</topic><topic>isoelectric point</topic><topic>Miscellaneous</topic><topic>Mission oriented research</topic><topic>molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>molecular weight</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>signal peptide</topic><topic>Southern blotting</topic><topic>Stenotrophomonas maltophilia</topic><topic>Stenotrophomonas maltophilia - enzymology</topic><topic>Stenotrophomonas maltophilia - genetics</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Neumann, S</creatorcontrib><creatorcontrib>Kula, M.R</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 Complete database</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</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 Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>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>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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>Neumann, S</au><au>Kula, M.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia</atitle><jtitle>Applied microbiology and biotechnology</jtitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2002-05-01</date><risdate>2002</risdate><volume>58</volume><issue>6</issue><spage>772</spage><epage>780</epage><pages>772-780</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>The peptide amidase (Pam) from the gram-negative bacterium Stenotrophomonas maltophilia catalyzes predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Its gene (pam) was isolated by Southern hybridization using a DNA probe derived from the known terminal amino acid sequence. Pam is a member of the amidase signature family and was identified as a periplasmic protein by an N-terminal signal peptide found in the gene. The processed protein consists of 503 amino acids with a molecular mass of 53.5 kDa. The recombinant enzyme with a C-terminal His6 tag has a monomeric structure and its isoelectric point is 6.3. The dipeptide amide L-Ala-L-Phe-NH2 is hydrolyzed in the absence of cofactors to L-Ala-L-Phe-OH and ammonia with V(max)=194 U/mg and K(m) <0.5 mM. The natural function of Pam remains unclear. Chymostatin (K(i)<0.3 micromolar) and Pefabloc SC (K(i) not determined) were identified as inhibitors. When the gene was expressed in Escherichia coli on a 12-l scale, the specific activity in the crude extract was 60 U/mg, compared to 0.24 U/mg in S. maltophilia. In the expression system, Pam made up about 31% of the total soluble cell protein. From 75 g wet cells, 2.1 g of >95% pure enzyme was obtained, which corresponds to a total activity of 416,000 units.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>12021798</pmid><doi>10.1007/s00253-002-0943-6</doi><tpages>9</tpages></addata></record> |
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| subjects | amidase Amides Amidohydrolases - chemistry Amidohydrolases - genetics Amidohydrolases - isolation & purification Amidohydrolases - metabolism Amino Acid Sequence Amino acids ammonia Bacteria Base Sequence Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Chromatography, Gel Cloning Cloning, Molecular DNA DNA Probes E coli Electrophoresis, Polyacrylamide Gel Enzyme Inhibitors - pharmacology Enzymes Escherichia coli Fundamental and applied biological sciences. Psychology gene overexpression genes Gram-negative bacteria hydrolysis isoelectric point Miscellaneous Mission oriented research molecular cloning Molecular Sequence Data molecular weight Peptides Proteins Sequence Homology, Amino Acid signal peptide Southern blotting Stenotrophomonas maltophilia Stenotrophomonas maltophilia - enzymology Stenotrophomonas maltophilia - genetics Substrate Specificity |
| title | Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia |
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