Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit
The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the...
Gespeichert in:
| Veröffentlicht in: | European journal of biochemistry 1990-08, Vol.192 (1), p.161-166 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 166 |
|---|---|
| container_issue | 1 |
| container_start_page | 161 |
| container_title | European journal of biochemistry |
| container_volume | 192 |
| creator | Hupperich, M Henschen, A Eggerer, H |
| description | The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the subunit are present as cysteines and not involved in disulfide bridges. The sequence shows no homology to known sequences of proteins or nucleic acids and reads (sequence; see text) |
| doi_str_mv | 10.1111/j.1432-1033.1990.tb19209.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80003680</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>80003680</sourcerecordid><originalsourceid>FETCH-LOGICAL-c288t-12a78893ba3a966b4c597d4529e85e83f88210a55afeba16fbee099e23dd6ad33</originalsourceid><addsrcrecordid>eNqFkU9PwzAMxSMEGmPwEZAiDtxanGTpEm5o4p-YxGWco6R1Rad2LUkqsW9Pq1W74osP_tnWe4-QOwYpG-phl7Kl4AkDIVKmNaTRMc1Bp79nZH4anZM5AFsmXMvsklyFsAOATGerGZlxDlICzIlbV9HbiLQ-2IC09G1DP2p0ocK6trTbY9-0-8piSrffSPO26Woc8M5XjfUHGqLv89h7pG1J40DY_FBPx0Lv-n0Vr8lFaeuAN1NfkK-X5-36Ldl8vr6vnzZJzpWKCeN2pZQWzgqrs8wtc6lXxVJyjUqiEqVSnIGV0pboLMtKhwhaIxdFkdlCiAW5P97tfPvTY4imqUI-ythj2wejBvkiU_AvyKQCrtlqAB-PYO7bEDyWZpJtGJgxCbMzo91mtNuMSZgpCfM7LN9OX3rXYHFanawXf1WthxM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15802917</pqid></control><display><type>article</type><title>Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Hupperich, M ; Henschen, A ; Eggerer, H</creator><creatorcontrib>Hupperich, M ; Henschen, A ; Eggerer, H</creatorcontrib><description>The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the subunit are present as cysteines and not involved in disulfide bridges. The sequence shows no homology to known sequences of proteins or nucleic acids and reads (sequence; see text)</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1990.tb19209.x</identifier><identifier>PMID: 2205500</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; citrate (pro-3S)-lyase ; Cyanogen Bromide - metabolism ; Disulfides ; Endopeptidases - metabolism ; Metalloendopeptidases ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes ; Oxo-Acid-Lyases ; Peptide Mapping ; Peptides - isolation & purification ; Peptides - metabolism ; Sulfhydryl Compounds ; Trypsin - metabolism</subject><ispartof>European journal of biochemistry, 1990-08, Vol.192 (1), p.161-166</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c288t-12a78893ba3a966b4c597d4529e85e83f88210a55afeba16fbee099e23dd6ad33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2205500$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hupperich, M</creatorcontrib><creatorcontrib>Henschen, A</creatorcontrib><creatorcontrib>Eggerer, H</creatorcontrib><title>Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the subunit are present as cysteines and not involved in disulfide bridges. The sequence shows no homology to known sequences of proteins or nucleic acids and reads (sequence; see text)</description><subject>Amino Acid Sequence</subject><subject>citrate (pro-3S)-lyase</subject><subject>Cyanogen Bromide - metabolism</subject><subject>Disulfides</subject><subject>Endopeptidases - metabolism</subject><subject>Metalloendopeptidases</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Multienzyme Complexes</subject><subject>Oxo-Acid-Lyases</subject><subject>Peptide Mapping</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - metabolism</subject><subject>Sulfhydryl Compounds</subject><subject>Trypsin - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9PwzAMxSMEGmPwEZAiDtxanGTpEm5o4p-YxGWco6R1Rad2LUkqsW9Pq1W74osP_tnWe4-QOwYpG-phl7Kl4AkDIVKmNaTRMc1Bp79nZH4anZM5AFsmXMvsklyFsAOATGerGZlxDlICzIlbV9HbiLQ-2IC09G1DP2p0ocK6trTbY9-0-8piSrffSPO26Woc8M5XjfUHGqLv89h7pG1J40DY_FBPx0Lv-n0Vr8lFaeuAN1NfkK-X5-36Ldl8vr6vnzZJzpWKCeN2pZQWzgqrs8wtc6lXxVJyjUqiEqVSnIGV0pboLMtKhwhaIxdFkdlCiAW5P97tfPvTY4imqUI-ythj2wejBvkiU_AvyKQCrtlqAB-PYO7bEDyWZpJtGJgxCbMzo91mtNuMSZgpCfM7LN9OX3rXYHFanawXf1WthxM</recordid><startdate>19900828</startdate><enddate>19900828</enddate><creator>Hupperich, M</creator><creator>Henschen, A</creator><creator>Eggerer, H</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900828</creationdate><title>Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit</title><author>Hupperich, M ; Henschen, A ; Eggerer, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c288t-12a78893ba3a966b4c597d4529e85e83f88210a55afeba16fbee099e23dd6ad33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>citrate (pro-3S)-lyase</topic><topic>Cyanogen Bromide - metabolism</topic><topic>Disulfides</topic><topic>Endopeptidases - metabolism</topic><topic>Metalloendopeptidases</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Multienzyme Complexes</topic><topic>Oxo-Acid-Lyases</topic><topic>Peptide Mapping</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>Sulfhydryl Compounds</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hupperich, M</creatorcontrib><creatorcontrib>Henschen, A</creatorcontrib><creatorcontrib>Eggerer, H</creatorcontrib><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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hupperich, M</au><au>Henschen, A</au><au>Eggerer, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1990-08-28</date><risdate>1990</risdate><volume>192</volume><issue>1</issue><spage>161</spage><epage>166</epage><pages>161-166</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the subunit are present as cysteines and not involved in disulfide bridges. The sequence shows no homology to known sequences of proteins or nucleic acids and reads (sequence; see text)</abstract><cop>England</cop><pmid>2205500</pmid><doi>10.1111/j.1432-1033.1990.tb19209.x</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1990-08, Vol.192 (1), p.161-166 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80003680 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence citrate (pro-3S)-lyase Cyanogen Bromide - metabolism Disulfides Endopeptidases - metabolism Metalloendopeptidases Molecular Sequence Data Molecular Weight Multienzyme Complexes Oxo-Acid-Lyases Peptide Mapping Peptides - isolation & purification Peptides - metabolism Sulfhydryl Compounds Trypsin - metabolism |
| title | Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T06%3A08%3A22IST&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=Citrate%20lyase%20from%20Klebsiella%20pneumoniae.%20The%20complete%20primary%20structure%20of%20the%20acyl%20lyase%20subunit&rft.jtitle=European%20journal%20of%20biochemistry&rft.au=Hupperich,%20M&rft.date=1990-08-28&rft.volume=192&rft.issue=1&rft.spage=161&rft.epage=166&rft.pages=161-166&rft.issn=0014-2956&rft.eissn=1432-1033&rft_id=info:doi/10.1111/j.1432-1033.1990.tb19209.x&rft_dat=%3Cproquest_cross%3E80003680%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=15802917&rft_id=info:pmid/2205500&rfr_iscdi=true |