A New Family of Phosphotransferases with a P-loop Motif
In most Gram-positive bacteria, catabolite repression is mediated by a bifunctional enzyme, the histidine-containing protein kinase/phosphatase (HprK/P). Based either on its primary sequence or on its recently solved three-dimensional structure, no straightforward homology with other known proteins...
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Veröffentlicht in: | The Journal of biological chemistry 2002-03, Vol.277 (13), p.11362-11367 |
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creator | Galinier, Anne Lavergne, Jean-Pierre Geourjon, Christophe Fieulaine, Sonia Nessler, Sylvie Jault, Jean-Michel |
description | In most Gram-positive bacteria, catabolite repression is mediated by a bifunctional enzyme, the histidine-containing protein kinase/phosphatase (HprK/P). Based either on its primary sequence or on its recently solved three-dimensional structure, no straightforward homology with other known proteins was found. However, we showed here that HprK/P exhibits a restricted homology with an unrelated phosphotransferase, the phosphoenolpyruvate carboxykinase. This includes notably two consecutive Asp residues from the phosphoenolpyruvate carboxykinase active site, whose equivalent residues were mutated in Bacillus subtilis HprK/P. Characterization of the corresponding mutants emphasizes the crucial role of these Asp residues in the HprK/P functioning. Furthermore, superimposition of HprK/P and phosphoenolpyruvate carboxykinase active sites supports the view that both enzymes bear significant resemblance in their overall mechanism of functioning showing that these two enzymes constitute a new family of phosphotransferases. |
doi_str_mv | 10.1074/jbc.M109527200 |
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Based either on its primary sequence or on its recently solved three-dimensional structure, no straightforward homology with other known proteins was found. However, we showed here that HprK/P exhibits a restricted homology with an unrelated phosphotransferase, the phosphoenolpyruvate carboxykinase. This includes notably two consecutive Asp residues from the phosphoenolpyruvate carboxykinase active site, whose equivalent residues were mutated in Bacillus subtilis HprK/P. Characterization of the corresponding mutants emphasizes the crucial role of these Asp residues in the HprK/P functioning. Furthermore, superimposition of HprK/P and phosphoenolpyruvate carboxykinase active sites supports the view that both enzymes bear significant resemblance in their overall mechanism of functioning showing that these two enzymes constitute a new family of phosphotransferases.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M109527200</identifier><identifier>PMID: 11796714</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Bacillus subtilis ; Bacteria - enzymology ; Biochemistry, Molecular Biology ; histidine-containing protein kinase/phosphatase ; Kinetics ; Life Sciences ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; phosphoenolpyruvate carboxykinase (ATP) ; phosphotransferase ; Phosphotransferases - chemistry ; Phosphotransferases - genetics ; Phosphotransferases - metabolism ; Protein Conformation ; Sequence Homology, Amino Acid ; Substrate Specificity</subject><ispartof>The Journal of biological chemistry, 2002-03, Vol.277 (13), p.11362-11367</ispartof><rights>2002 © 2002 ASBMB. 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Based either on its primary sequence or on its recently solved three-dimensional structure, no straightforward homology with other known proteins was found. However, we showed here that HprK/P exhibits a restricted homology with an unrelated phosphotransferase, the phosphoenolpyruvate carboxykinase. This includes notably two consecutive Asp residues from the phosphoenolpyruvate carboxykinase active site, whose equivalent residues were mutated in Bacillus subtilis HprK/P. Characterization of the corresponding mutants emphasizes the crucial role of these Asp residues in the HprK/P functioning. Furthermore, superimposition of HprK/P and phosphoenolpyruvate carboxykinase active sites supports the view that both enzymes bear significant resemblance in their overall mechanism of functioning showing that these two enzymes constitute a new family of phosphotransferases.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Bacillus subtilis</subject><subject>Bacteria - enzymology</subject><subject>Biochemistry, Molecular Biology</subject><subject>histidine-containing protein kinase/phosphatase</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>phosphoenolpyruvate carboxykinase (ATP)</subject><subject>phosphotransferase</subject><subject>Phosphotransferases - chemistry</subject><subject>Phosphotransferases - genetics</subject><subject>Phosphotransferases - metabolism</subject><subject>Protein Conformation</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1rGzEQhkVpaBy31x7LHkohh3VHH2utjibUccBOcmihN6HVjroKu5YrrWPy76Ngk5wyl4HheV-Gh5CvFGYUpPj50NjZhoKqmGQAH8iEQs1LXtG_H8kEgNFSsao-JxcpPUAeoegnck6pVHNJxYTIRXGLh2JpBt8_FcEV911Iuy6M0WyTw2gSpuLgx64wxX3Zh7ArNmH07jM5c6ZP-OW0p-TP8tfvq1W5vru-uVqsSyukGMvGSqydEhZbqJ21qpk7USPMjTMOGmE4CsRKtsrK1jCnkDEJXHBuVGNUy6fk8tjbmV7voh9MfNLBeL1arPXLDYBTAVX1SDP748juYvi_xzTqwSeLfW-2GPZJ05opoKLK4OwI2hhSiuhemynoF606a9VvWnPg26l53wzYvuEnjxn4fnrT_-sOPqJufLAdDppJqSnPJJ-zjNVHDLOyR49RJ-txm-3kiB11G_x7LzwDOBOQeA</recordid><startdate>20020329</startdate><enddate>20020329</enddate><creator>Galinier, Anne</creator><creator>Lavergne, Jean-Pierre</creator><creator>Geourjon, Christophe</creator><creator>Fieulaine, Sonia</creator><creator>Nessler, Sylvie</creator><creator>Jault, Jean-Michel</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-5988-016X</orcidid><orcidid>https://orcid.org/0000-0001-6365-4229</orcidid></search><sort><creationdate>20020329</creationdate><title>A New Family of Phosphotransferases with a P-loop Motif</title><author>Galinier, Anne ; Lavergne, Jean-Pierre ; Geourjon, Christophe ; Fieulaine, Sonia ; Nessler, Sylvie ; Jault, Jean-Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-bc7e8f94ced08fcc9b6f48e06afaf0b4a3e4ee57d9c7da2f9e22703433a9ba9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Bacillus subtilis</topic><topic>Bacteria - enzymology</topic><topic>Biochemistry, Molecular Biology</topic><topic>histidine-containing protein kinase/phosphatase</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>phosphoenolpyruvate carboxykinase (ATP)</topic><topic>phosphotransferase</topic><topic>Phosphotransferases - chemistry</topic><topic>Phosphotransferases - genetics</topic><topic>Phosphotransferases - metabolism</topic><topic>Protein Conformation</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Galinier, Anne</creatorcontrib><creatorcontrib>Lavergne, Jean-Pierre</creatorcontrib><creatorcontrib>Geourjon, Christophe</creatorcontrib><creatorcontrib>Fieulaine, Sonia</creatorcontrib><creatorcontrib>Nessler, Sylvie</creatorcontrib><creatorcontrib>Jault, Jean-Michel</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Galinier, Anne</au><au>Lavergne, Jean-Pierre</au><au>Geourjon, Christophe</au><au>Fieulaine, Sonia</au><au>Nessler, Sylvie</au><au>Jault, Jean-Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A New Family of Phosphotransferases with a P-loop Motif</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-03-29</date><risdate>2002</risdate><volume>277</volume><issue>13</issue><spage>11362</spage><epage>11367</epage><pages>11362-11367</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>In most Gram-positive bacteria, catabolite repression is mediated by a bifunctional enzyme, the histidine-containing protein kinase/phosphatase (HprK/P). Based either on its primary sequence or on its recently solved three-dimensional structure, no straightforward homology with other known proteins was found. However, we showed here that HprK/P exhibits a restricted homology with an unrelated phosphotransferase, the phosphoenolpyruvate carboxykinase. This includes notably two consecutive Asp residues from the phosphoenolpyruvate carboxykinase active site, whose equivalent residues were mutated in Bacillus subtilis HprK/P. Characterization of the corresponding mutants emphasizes the crucial role of these Asp residues in the HprK/P functioning. 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subjects | Amino Acid Motifs Amino Acid Sequence Bacillus subtilis Bacteria - enzymology Biochemistry, Molecular Biology histidine-containing protein kinase/phosphatase Kinetics Life Sciences Molecular Sequence Data Mutagenesis, Site-Directed phosphoenolpyruvate carboxykinase (ATP) phosphotransferase Phosphotransferases - chemistry Phosphotransferases - genetics Phosphotransferases - metabolism Protein Conformation Sequence Homology, Amino Acid Substrate Specificity |
title | A New Family of Phosphotransferases with a P-loop Motif |
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