Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661
Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid. Transaminases are involved in amino acid metabolism in all organisms. Enzymes of this superfamily are widely used to develop biocatalysts for the...
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Veröffentlicht in: | Crystallography reports 2021-09, Vol.66 (5), p.802-807 |
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creator | Boyko, K. M. Nikolaeva, A. Yu Bakunova, A. K. Stekhanova, T. N. Rakitina, T. V. Popov, V. O. Bezsudnova, E. Yu |
description | Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid. Transaminases are involved in amino acid metabolism in all organisms. Enzymes of this superfamily are widely used to develop biocatalysts for the stereoselective amination of organic compounds for fine organic synthesis. The brief biochemical characterization of thermostable fold type I PLP-dependent transaminase from the thermophilic archaeon
Methanocaldococcus jannaschii
DSM 2661 is reported. The crystal structure of this enzyme was determined at 1.8 Å resolution. The structure of the functional dimer of the enzyme and the organization of its active site are compared with those of the close homologs. |
doi_str_mv | 10.1134/S1063774521050035 |
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Methanocaldococcus jannaschii
DSM 2661 is reported. The crystal structure of this enzyme was determined at 1.8 Å resolution. The structure of the functional dimer of the enzyme and the organization of its active site are compared with those of the close homologs.</description><identifier>ISSN: 1063-7745</identifier><identifier>EISSN: 1562-689X</identifier><identifier>DOI: 10.1134/S1063774521050035</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Amino acids ; Crystal structure ; Crystallography and Scattering Methods ; Dimers ; Enzymes ; Homology ; Molecular structure ; Organic compounds ; Physics ; Physics and Astronomy ; Stereoselectivity ; Structure of Macromolecular Compounds ; Transaminases</subject><ispartof>Crystallography reports, 2021-09, Vol.66 (5), p.802-807</ispartof><rights>Pleiades Publishing, Inc. 2021. ISSN 1063-7745, Crystallography Reports, 2021, Vol. 66, No. 5, pp. 802–807. © Pleiades Publishing, Inc., 2021. Russian Text © The Author(s), 2021, published in Kristallografiya, 2021, Vol. 66, No. 5, pp. 776–781.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c268t-9c2674891dc91c69e338591d76a2a896a38b0877f522109359866cb978a76ff03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S1063774521050035$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S1063774521050035$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Boyko, K. M.</creatorcontrib><creatorcontrib>Nikolaeva, A. Yu</creatorcontrib><creatorcontrib>Bakunova, A. K.</creatorcontrib><creatorcontrib>Stekhanova, T. N.</creatorcontrib><creatorcontrib>Rakitina, T. V.</creatorcontrib><creatorcontrib>Popov, V. O.</creatorcontrib><creatorcontrib>Bezsudnova, E. Yu</creatorcontrib><title>Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661</title><title>Crystallography reports</title><addtitle>Crystallogr. Rep</addtitle><description>Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid. Transaminases are involved in amino acid metabolism in all organisms. Enzymes of this superfamily are widely used to develop biocatalysts for the stereoselective amination of organic compounds for fine organic synthesis. The brief biochemical characterization of thermostable fold type I PLP-dependent transaminase from the thermophilic archaeon
Methanocaldococcus jannaschii
DSM 2661 is reported. The crystal structure of this enzyme was determined at 1.8 Å resolution. The structure of the functional dimer of the enzyme and the organization of its active site are compared with those of the close homologs.</description><subject>Amino acids</subject><subject>Crystal structure</subject><subject>Crystallography and Scattering Methods</subject><subject>Dimers</subject><subject>Enzymes</subject><subject>Homology</subject><subject>Molecular structure</subject><subject>Organic compounds</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Stereoselectivity</subject><subject>Structure of Macromolecular Compounds</subject><subject>Transaminases</subject><issn>1063-7745</issn><issn>1562-689X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp1ULtOwzAUtRBIlMIHsFliDvgRv8ao5SW1YkiQ2CLXdUiqxC52MrDw7bgqEgNiOvfoPKRzAbjG6BZjmt-VGHEqRM4IRgwhyk7ADDNOMi7V22m6k5wd9HNwEeMOISQlzmfgq2qDtdmyG6yLnXe6h-UYJjNOwULfwKq1YfBx1JvewmVWDJ3zsDDdFlZBu6gT19HCJvgBjq2FRTCttt7BtR1b7bzR_dYbb8wU4U67ZDZt18FluYaEc3wJzhrdR3v1g3Pw-nBfLZ6y1cvj86JYZYZwOWYqgcilwlujsOHKUipZYoJroqXimsoNkkI0jKT9ijIlOTcbJaQWvGkQnYObY-8--I_JxrHe-SmktbEmTCiqmMgPLnx0meBjDLap96EbdPisMaoPb67_vDllyDETk9e92_Db_H_oG3bnfc8</recordid><startdate>20210901</startdate><enddate>20210901</enddate><creator>Boyko, K. M.</creator><creator>Nikolaeva, A. Yu</creator><creator>Bakunova, A. K.</creator><creator>Stekhanova, T. N.</creator><creator>Rakitina, T. V.</creator><creator>Popov, V. O.</creator><creator>Bezsudnova, E. Yu</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20210901</creationdate><title>Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661</title><author>Boyko, K. M. ; Nikolaeva, A. Yu ; Bakunova, A. K. ; Stekhanova, T. N. ; Rakitina, T. V. ; Popov, V. O. ; Bezsudnova, E. Yu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c268t-9c2674891dc91c69e338591d76a2a896a38b0877f522109359866cb978a76ff03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino acids</topic><topic>Crystal structure</topic><topic>Crystallography and Scattering Methods</topic><topic>Dimers</topic><topic>Enzymes</topic><topic>Homology</topic><topic>Molecular structure</topic><topic>Organic compounds</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Stereoselectivity</topic><topic>Structure of Macromolecular Compounds</topic><topic>Transaminases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boyko, K. M.</creatorcontrib><creatorcontrib>Nikolaeva, A. Yu</creatorcontrib><creatorcontrib>Bakunova, A. K.</creatorcontrib><creatorcontrib>Stekhanova, T. N.</creatorcontrib><creatorcontrib>Rakitina, T. V.</creatorcontrib><creatorcontrib>Popov, V. O.</creatorcontrib><creatorcontrib>Bezsudnova, E. Yu</creatorcontrib><collection>CrossRef</collection><jtitle>Crystallography reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boyko, K. M.</au><au>Nikolaeva, A. Yu</au><au>Bakunova, A. K.</au><au>Stekhanova, T. N.</au><au>Rakitina, T. V.</au><au>Popov, V. O.</au><au>Bezsudnova, E. Yu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661</atitle><jtitle>Crystallography reports</jtitle><stitle>Crystallogr. Rep</stitle><date>2021-09-01</date><risdate>2021</risdate><volume>66</volume><issue>5</issue><spage>802</spage><epage>807</epage><pages>802-807</pages><issn>1063-7745</issn><eissn>1562-689X</eissn><abstract>Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid. Transaminases are involved in amino acid metabolism in all organisms. Enzymes of this superfamily are widely used to develop biocatalysts for the stereoselective amination of organic compounds for fine organic synthesis. The brief biochemical characterization of thermostable fold type I PLP-dependent transaminase from the thermophilic archaeon
Methanocaldococcus jannaschii
DSM 2661 is reported. The crystal structure of this enzyme was determined at 1.8 Å resolution. The structure of the functional dimer of the enzyme and the organization of its active site are compared with those of the close homologs.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S1063774521050035</doi><tpages>6</tpages></addata></record> |
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subjects | Amino acids Crystal structure Crystallography and Scattering Methods Dimers Enzymes Homology Molecular structure Organic compounds Physics Physics and Astronomy Stereoselectivity Structure of Macromolecular Compounds Transaminases |
title | Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661 |
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