Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate
Aspartate aminotransferase (EC 2.6.1.1; L-aspartate: 2-oxoglutarate aminotransferase, AATase) is one of the key enzymes of nitrogen metabolism. The tissues of vertebrates contain 2 homologous isozymic forms of this enzyme: a cytosolic and mitochondrial form. Both isoenzymes are dimeric proteins, con...
Gespeichert in:
Veröffentlicht in: | FEBS letters 1982-02, Vol.138 (1), p.113-116 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 116 |
---|---|
container_issue | 1 |
container_start_page | 113 |
container_title | FEBS letters |
container_volume | 138 |
creator | Harutyunyan, E.G. Malashkevich, V.N. Tersyan, S.S. Kochkina, V.M. Torchinsky, Yu.M. Braunstein, A.E. |
description | Aspartate aminotransferase (EC 2.6.1.1; L-aspartate: 2-oxoglutarate aminotransferase, AATase) is one of the key enzymes of nitrogen metabolism. The tissues of vertebrates contain 2 homologous isozymic forms of this enzyme: a cytosolic and mitochondrial form. Both isoenzymes are dimeric proteins, consisting of 2 identical subunits of M sub(r) similar to 45,000. Currently, X-ray structural investigations are underway of chicken cAATase and mAATase and of porcine cAATase. Here, the authors report studies of the three-dimensional structure of chicken cAATase at 3.2 angstrom resolution. |
doi_str_mv | 10.1016/0014-5793(82)80407-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_74025971</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579382804079</els_id><sourcerecordid>74025971</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4129-ed73a4cceb6027e14feb2cab7ca80f7ac6d8ade15b6b7c7fea4e3facd9f5829f3</originalsourceid><addsrcrecordid>eNqNkcFuFSEYhYnR1Gv1DTRhZXQxFRhmgI1JbXrVpImbuiYM8-OgM8MVGNv7AG59KV9MpvemS3VF_v9850A4CD2n5IwS2r4hhPKqEap-JdlrSTgRlXqANlSKuqp5Kx-izT3yGD1J6Ssps6TqBJ0I0grJ2g36dT1EgKr3E8zJh9mMOOW42LxEwCbj-ozh3z9xhBTGJRcAB4fzANiGaTfC7TrafQ5F9habtDMxm1ysk59DjmZODqJJgF0ME7aDt99gxgMUDN_4PGBWhdvwpWSbWHxP0SNnxgTPjucp-ry9vL74UF19ev_x4vyqspwyVUEvasOtha4lTADlDjpmTSeskcQJY9temh5o07VlJxwYDrUztleukUy5-hS9POTuYvi-QMp68snCOJoZwpK04IQ1StB_grThitJGFJAfQBtDShGc3kU_mbjXlOi1L72WodcytGT6ri-tiu3FMX_pJujvTceCir496Dd-hP1_Zert5Tu2CutesrvtetHbQxCUb_3hIepkPcwWeh_BZt0H__eX_gEj2rzk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15491157</pqid></control><display><type>article</type><title>Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Harutyunyan, E.G. ; Malashkevich, V.N. ; Tersyan, S.S. ; Kochkina, V.M. ; Torchinsky, Yu.M. ; Braunstein, A.E.</creator><creatorcontrib>Harutyunyan, E.G. ; Malashkevich, V.N. ; Tersyan, S.S. ; Kochkina, V.M. ; Torchinsky, Yu.M. ; Braunstein, A.E.</creatorcontrib><description>Aspartate aminotransferase (EC 2.6.1.1; L-aspartate: 2-oxoglutarate aminotransferase, AATase) is one of the key enzymes of nitrogen metabolism. The tissues of vertebrates contain 2 homologous isozymic forms of this enzyme: a cytosolic and mitochondrial form. Both isoenzymes are dimeric proteins, consisting of 2 identical subunits of M sub(r) similar to 45,000. Currently, X-ray structural investigations are underway of chicken cAATase and mAATase and of porcine cAATase. Here, the authors report studies of the three-dimensional structure of chicken cAATase at 3.2 angstrom resolution.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(82)80407-9</identifier><identifier>PMID: 7067826</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>2-oxoglutaric acid ; Animals ; aspartate aminotransferase ; Aspartate Aminotransferases - metabolism ; cAATase, cytosolic aspartate aminotransferase ; Chickens ; cytosol ; DTNB, 5,5'-dithiobis-(2-nitrobenzoate) ; heart ; Ketoglutaric Acids - metabolism ; mAATase, mitochondrial aspartate aminotransferase ; MMA, methylmercuriacetate ; Models, Molecular ; Models, Structural ; Myocardium - enzymology ; p-CMB, p-chloromercuribenzoate ; PLP, pyridoxal-5′-phosphate ; X-ray diffraction</subject><ispartof>FEBS letters, 1982-02, Vol.138 (1), p.113-116</ispartof><rights>1982</rights><rights>FEBS Letters 138 (1982) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4129-ed73a4cceb6027e14feb2cab7ca80f7ac6d8ade15b6b7c7fea4e3facd9f5829f3</citedby><cites>FETCH-LOGICAL-c4129-ed73a4cceb6027e14feb2cab7ca80f7ac6d8ade15b6b7c7fea4e3facd9f5829f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(82)80407-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7067826$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harutyunyan, E.G.</creatorcontrib><creatorcontrib>Malashkevich, V.N.</creatorcontrib><creatorcontrib>Tersyan, S.S.</creatorcontrib><creatorcontrib>Kochkina, V.M.</creatorcontrib><creatorcontrib>Torchinsky, Yu.M.</creatorcontrib><creatorcontrib>Braunstein, A.E.</creatorcontrib><title>Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Aspartate aminotransferase (EC 2.6.1.1; L-aspartate: 2-oxoglutarate aminotransferase, AATase) is one of the key enzymes of nitrogen metabolism. The tissues of vertebrates contain 2 homologous isozymic forms of this enzyme: a cytosolic and mitochondrial form. Both isoenzymes are dimeric proteins, consisting of 2 identical subunits of M sub(r) similar to 45,000. Currently, X-ray structural investigations are underway of chicken cAATase and mAATase and of porcine cAATase. Here, the authors report studies of the three-dimensional structure of chicken cAATase at 3.2 angstrom resolution.</description><subject>2-oxoglutaric acid</subject><subject>Animals</subject><subject>aspartate aminotransferase</subject><subject>Aspartate Aminotransferases - metabolism</subject><subject>cAATase, cytosolic aspartate aminotransferase</subject><subject>Chickens</subject><subject>cytosol</subject><subject>DTNB, 5,5'-dithiobis-(2-nitrobenzoate)</subject><subject>heart</subject><subject>Ketoglutaric Acids - metabolism</subject><subject>mAATase, mitochondrial aspartate aminotransferase</subject><subject>MMA, methylmercuriacetate</subject><subject>Models, Molecular</subject><subject>Models, Structural</subject><subject>Myocardium - enzymology</subject><subject>p-CMB, p-chloromercuribenzoate</subject><subject>PLP, pyridoxal-5′-phosphate</subject><subject>X-ray diffraction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFuFSEYhYnR1Gv1DTRhZXQxFRhmgI1JbXrVpImbuiYM8-OgM8MVGNv7AG59KV9MpvemS3VF_v9850A4CD2n5IwS2r4hhPKqEap-JdlrSTgRlXqANlSKuqp5Kx-izT3yGD1J6Ssps6TqBJ0I0grJ2g36dT1EgKr3E8zJh9mMOOW42LxEwCbj-ozh3z9xhBTGJRcAB4fzANiGaTfC7TrafQ5F9habtDMxm1ysk59DjmZODqJJgF0ME7aDt99gxgMUDN_4PGBWhdvwpWSbWHxP0SNnxgTPjucp-ry9vL74UF19ev_x4vyqspwyVUEvasOtha4lTADlDjpmTSeskcQJY9temh5o07VlJxwYDrUztleukUy5-hS9POTuYvi-QMp68snCOJoZwpK04IQ1StB_grThitJGFJAfQBtDShGc3kU_mbjXlOi1L72WodcytGT6ri-tiu3FMX_pJujvTceCir496Dd-hP1_Zert5Tu2CutesrvtetHbQxCUb_3hIepkPcwWeh_BZt0H__eX_gEj2rzk</recordid><startdate>19820208</startdate><enddate>19820208</enddate><creator>Harutyunyan, E.G.</creator><creator>Malashkevich, V.N.</creator><creator>Tersyan, S.S.</creator><creator>Kochkina, V.M.</creator><creator>Torchinsky, Yu.M.</creator><creator>Braunstein, A.E.</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>19820208</creationdate><title>Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate</title><author>Harutyunyan, E.G. ; Malashkevich, V.N. ; Tersyan, S.S. ; Kochkina, V.M. ; Torchinsky, Yu.M. ; Braunstein, A.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4129-ed73a4cceb6027e14feb2cab7ca80f7ac6d8ade15b6b7c7fea4e3facd9f5829f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>2-oxoglutaric acid</topic><topic>Animals</topic><topic>aspartate aminotransferase</topic><topic>Aspartate Aminotransferases - metabolism</topic><topic>cAATase, cytosolic aspartate aminotransferase</topic><topic>Chickens</topic><topic>cytosol</topic><topic>DTNB, 5,5'-dithiobis-(2-nitrobenzoate)</topic><topic>heart</topic><topic>Ketoglutaric Acids - metabolism</topic><topic>mAATase, mitochondrial aspartate aminotransferase</topic><topic>MMA, methylmercuriacetate</topic><topic>Models, Molecular</topic><topic>Models, Structural</topic><topic>Myocardium - enzymology</topic><topic>p-CMB, p-chloromercuribenzoate</topic><topic>PLP, pyridoxal-5′-phosphate</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Harutyunyan, E.G.</creatorcontrib><creatorcontrib>Malashkevich, V.N.</creatorcontrib><creatorcontrib>Tersyan, S.S.</creatorcontrib><creatorcontrib>Kochkina, V.M.</creatorcontrib><creatorcontrib>Torchinsky, Yu.M.</creatorcontrib><creatorcontrib>Braunstein, A.E.</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Harutyunyan, E.G.</au><au>Malashkevich, V.N.</au><au>Tersyan, S.S.</au><au>Kochkina, V.M.</au><au>Torchinsky, Yu.M.</au><au>Braunstein, A.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1982-02-08</date><risdate>1982</risdate><volume>138</volume><issue>1</issue><spage>113</spage><epage>116</epage><pages>113-116</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Aspartate aminotransferase (EC 2.6.1.1; L-aspartate: 2-oxoglutarate aminotransferase, AATase) is one of the key enzymes of nitrogen metabolism. The tissues of vertebrates contain 2 homologous isozymic forms of this enzyme: a cytosolic and mitochondrial form. Both isoenzymes are dimeric proteins, consisting of 2 identical subunits of M sub(r) similar to 45,000. Currently, X-ray structural investigations are underway of chicken cAATase and mAATase and of porcine cAATase. Here, the authors report studies of the three-dimensional structure of chicken cAATase at 3.2 angstrom resolution.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7067826</pmid><doi>10.1016/0014-5793(82)80407-9</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0014-5793 |
ispartof | FEBS letters, 1982-02, Vol.138 (1), p.113-116 |
issn | 0014-5793 1873-3468 |
language | eng |
recordid | cdi_proquest_miscellaneous_74025971 |
source | MEDLINE; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | 2-oxoglutaric acid Animals aspartate aminotransferase Aspartate Aminotransferases - metabolism cAATase, cytosolic aspartate aminotransferase Chickens cytosol DTNB, 5,5'-dithiobis-(2-nitrobenzoate) heart Ketoglutaric Acids - metabolism mAATase, mitochondrial aspartate aminotransferase MMA, methylmercuriacetate Models, Molecular Models, Structural Myocardium - enzymology p-CMB, p-chloromercuribenzoate PLP, pyridoxal-5′-phosphate X-ray diffraction |
title | Three-dimensional structure at 3.2 Å resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T00%3A46%3A41IST&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=Three-dimensional%20structure%20at%203.2%20%C3%85%20resolution%20of%20the%20complex%20of%20cytosolic%20aspartate%20aminotransferase%20from%20chicken%20heart%20with%202-oxoglutarate&rft.jtitle=FEBS%20letters&rft.au=Harutyunyan,%20E.G.&rft.date=1982-02-08&rft.volume=138&rft.issue=1&rft.spage=113&rft.epage=116&rft.pages=113-116&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/0014-5793(82)80407-9&rft_dat=%3Cproquest_cross%3E74025971%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=15491157&rft_id=info:pmid/7067826&rft_els_id=0014579382804079&rfr_iscdi=true |