A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l‐homoserine O‐acetyl transferases
MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β‐hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle...
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| Veröffentlicht in: | FEBS letters 2016-01, Vol.590 (1), p.174-184 |
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| creator | Tölzer, Christine Pal, Sonia Watzlawick, Hildegard Altenbuchner, Josef Niefind, Karsten Ferguson, Stuart |
| description | MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β‐hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x‐ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl‐CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter. |
| doi_str_mv | 10.1002/1873-3468.12031 |
| format | Article |
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Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x‐ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl‐CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.12031</identifier><identifier>PMID: 26787467</identifier><language>eng</language><publisher>England</publisher><subject>Acetyl Coenzyme A - chemistry ; Acetyl Coenzyme A - metabolism ; acetyl ester hydrolysis ; Acetyltransferases - chemistry ; Acetyltransferases - classification ; Acetyltransferases - metabolism ; Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Binding Sites ; Catalytic Domain ; Conserved Sequence ; crystal structure ; Crystallography, X-Ray ; Databases, Protein ; esterase ; Esterases - chemistry ; Esterases - metabolism ; Homoserine - chemistry ; Homoserine - metabolism ; l‐homoserine O‐transacetylase ; methyl alkyl ketone degradation pathway ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Pseudomonas - enzymology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Structural Homology, Protein ; Substrate Specificity ; α/β‐hydrolase fold</subject><ispartof>FEBS letters, 2016-01, Vol.590 (1), p.174-184</ispartof><rights>2015 Federation of European Biochemical Societies</rights><rights>2015 Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3851-db133df22993de60b2bd41388378b24979c2bcca2216f1ed372cd87c75c1a1c53</citedby><cites>FETCH-LOGICAL-c3851-db133df22993de60b2bd41388378b24979c2bcca2216f1ed372cd87c75c1a1c53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1873-3468.12031$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1873-3468.12031$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,1428,27905,27906,45555,45556,46390,46814</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26787467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ferguson, Stuart</contributor><creatorcontrib>Tölzer, Christine</creatorcontrib><creatorcontrib>Pal, Sonia</creatorcontrib><creatorcontrib>Watzlawick, Hildegard</creatorcontrib><creatorcontrib>Altenbuchner, Josef</creatorcontrib><creatorcontrib>Niefind, Karsten</creatorcontrib><creatorcontrib>Ferguson, Stuart</creatorcontrib><title>A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l‐homoserine O‐acetyl transferases</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β‐hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x‐ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl‐CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.</description><subject>Acetyl Coenzyme A - chemistry</subject><subject>Acetyl Coenzyme A - metabolism</subject><subject>acetyl ester hydrolysis</subject><subject>Acetyltransferases - chemistry</subject><subject>Acetyltransferases - classification</subject><subject>Acetyltransferases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Catalytic Domain</subject><subject>Conserved Sequence</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Databases, Protein</subject><subject>esterase</subject><subject>Esterases - chemistry</subject><subject>Esterases - metabolism</subject><subject>Homoserine - chemistry</subject><subject>Homoserine - metabolism</subject><subject>l‐homoserine O‐transacetylase</subject><subject>methyl alkyl ketone degradation pathway</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Pseudomonas - enzymology</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structural Homology, Protein</subject><subject>Substrate Specificity</subject><subject>α/β‐hydrolase fold</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkTtO7DAUhi0EguFR0125pAnjRyZ2SkDDBQmJBmrLr8wEOTHXThiFiiWwADbBXQiLYCU4DNBSWef4O5_O0Q_AIUbHGCEyxZzRjOYFP8YEUbwBJj-dTTBBCOfZjJV0B-zGeIdSzXG5DXZIwTjLCzYBLyew9Q_WQRs7G2S0MPaqkk3tBriquyV8e52-_X9_el4OJng3ApV3JlGLxThioBpg7EKvuz7YCH0Fu5WHSuqkq2Xyto9Dkz6WvvHOL3wfYeehG42pExPUWnidSqltNzjYBdnG6nOVuA-2KumiPfh698Dt-fzm7CK7uv57eXZylWnKZzgzClNqKkLKkhpbIEWUyTHlnDKuSF6yUhOltSQEFxW2hjKiDWeazTSWWM_oHjhae--D_9ens0RTR22dk61NCwvMClQiwvmITteoDj7GYCtxH-pGhkFgJMZIxBiAGAMQn5GkiT9f8l411vzw3xkkoFgDq9rZ4TefOJ-fkrX5AwmwnhA</recordid><startdate>201601</startdate><enddate>201601</enddate><creator>Tölzer, Christine</creator><creator>Pal, Sonia</creator><creator>Watzlawick, Hildegard</creator><creator>Altenbuchner, Josef</creator><creator>Niefind, Karsten</creator><creator>Ferguson, Stuart</creator><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>7X8</scope></search><sort><creationdate>201601</creationdate><title>A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l‐homoserine O‐acetyl transferases</title><author>Tölzer, Christine ; Pal, Sonia ; Watzlawick, Hildegard ; Altenbuchner, Josef ; Niefind, Karsten ; Ferguson, Stuart</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3851-db133df22993de60b2bd41388378b24979c2bcca2216f1ed372cd87c75c1a1c53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acetyl Coenzyme A - chemistry</topic><topic>Acetyl Coenzyme A - metabolism</topic><topic>acetyl ester hydrolysis</topic><topic>Acetyltransferases - chemistry</topic><topic>Acetyltransferases - classification</topic><topic>Acetyltransferases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Catalytic Domain</topic><topic>Conserved Sequence</topic><topic>crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Databases, Protein</topic><topic>esterase</topic><topic>Esterases - chemistry</topic><topic>Esterases - metabolism</topic><topic>Homoserine - chemistry</topic><topic>Homoserine - metabolism</topic><topic>l‐homoserine O‐transacetylase</topic><topic>methyl alkyl ketone degradation pathway</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Pseudomonas - enzymology</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structural Homology, Protein</topic><topic>Substrate Specificity</topic><topic>α/β‐hydrolase fold</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tölzer, Christine</creatorcontrib><creatorcontrib>Pal, Sonia</creatorcontrib><creatorcontrib>Watzlawick, Hildegard</creatorcontrib><creatorcontrib>Altenbuchner, Josef</creatorcontrib><creatorcontrib>Niefind, Karsten</creatorcontrib><creatorcontrib>Ferguson, Stuart</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tölzer, Christine</au><au>Pal, Sonia</au><au>Watzlawick, Hildegard</au><au>Altenbuchner, Josef</au><au>Niefind, Karsten</au><au>Ferguson, Stuart</au><au>Ferguson, Stuart</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l‐homoserine O‐acetyl transferases</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2016-01</date><risdate>2016</risdate><volume>590</volume><issue>1</issue><spage>174</spage><epage>184</epage><pages>174-184</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β‐hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x‐ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl‐CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.</abstract><cop>England</cop><pmid>26787467</pmid><doi>10.1002/1873-3468.12031</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Alma/SFX Local Collection |
| subjects | Acetyl Coenzyme A - chemistry Acetyl Coenzyme A - metabolism acetyl ester hydrolysis Acetyltransferases - chemistry Acetyltransferases - classification Acetyltransferases - metabolism Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Catalytic Domain Conserved Sequence crystal structure Crystallography, X-Ray Databases, Protein esterase Esterases - chemistry Esterases - metabolism Homoserine - chemistry Homoserine - metabolism l‐homoserine O‐transacetylase methyl alkyl ketone degradation pathway Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding Protein Structure, Secondary Pseudomonas - enzymology Sequence Alignment Sequence Homology, Amino Acid Structural Homology, Protein Substrate Specificity α/β‐hydrolase fold |
| title | A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l‐homoserine O‐acetyl transferases |
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