The family of sarcosine oxidases: Same reaction, different products
The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subseq...
Gespeichert in:
Veröffentlicht in: | Archives of biochemistry and biophysics 2021-06, Vol.704, p.108868-108868, Article 108868 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 108868 |
---|---|
container_issue | |
container_start_page | 108868 |
container_title | Archives of biochemistry and biophysics |
container_volume | 704 |
creator | Lahham, Majd Jha, Shalinee Goj, Dominic Macheroux, Peter Wallner, Silvia |
description | The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subsequent spontaneous non-enzymatic reactions, forming an array of different products. These products range from demethylated simple species to complex alkaloids. The enzymes belonging to the sarcosine oxidase family, namely, monomeric and heterotetrameric sarcosine oxidase, l-pipecolate oxidase, N-methyltryptophan oxidase, NikD, l-proline dehydrogenase, FsqB, fructosamine oxidase and saccharopine oxidase have unique features differentiating them from other amine oxidases. This review highlights the key attributes of the sarcosine oxidase family enzymes, in terms of their substrate binding motif, type of oxidation reaction mediated and FAD regeneration, to define the boundaries of this group and demarcate these enzymes from other amine oxidase families. |
doi_str_mv | 10.1016/j.abb.2021.108868 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2508891306</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0003986121001181</els_id><sourcerecordid>2508891306</sourcerecordid><originalsourceid>FETCH-LOGICAL-c396t-6bdd702073a4e2825fad94094fe84bbab70d1306b780b4b00e716273b9e2aaa53</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwAWxQlixIGdup48AKVbykSiwoa8uPiXCVB9gJon9PqhSWrEYjnXtHcwg5pzCnQMX1Zq6NmTNgdNilFPKATCkUIgUus0MyBQCeFlLQCTmJcQNAaSbYMZlwLikrqJiS5fodk1LXvtombZlEHWwbfYNJ--2djhhvklddYxJQ2863zVXifFliwKZLPkLretvFU3JU6iri2X7OyNvD_Xr5lK5eHp-Xd6vU8kJ0qTDO5cAg5zpDJtmi1K7IoMhKlJkx2uTgKAdhcgkmMwCYU8FybgpkWusFn5HLsXc4_Nlj7FTto8Wq0g22fVRsMUgodhUDSkfUhjbGgKX6CL7WYasoqJ07tVGDO7Vzp0Z3Q-ZiX9-bGt1f4lfWANyOAA5PfnkMKlqPjUXnA9pOudb_U_8DeAx90g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2508891306</pqid></control><display><type>article</type><title>The family of sarcosine oxidases: Same reaction, different products</title><source>ScienceDirect Journals (5 years ago - present)</source><creator>Lahham, Majd ; Jha, Shalinee ; Goj, Dominic ; Macheroux, Peter ; Wallner, Silvia</creator><creatorcontrib>Lahham, Majd ; Jha, Shalinee ; Goj, Dominic ; Macheroux, Peter ; Wallner, Silvia</creatorcontrib><description>The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subsequent spontaneous non-enzymatic reactions, forming an array of different products. These products range from demethylated simple species to complex alkaloids. The enzymes belonging to the sarcosine oxidase family, namely, monomeric and heterotetrameric sarcosine oxidase, l-pipecolate oxidase, N-methyltryptophan oxidase, NikD, l-proline dehydrogenase, FsqB, fructosamine oxidase and saccharopine oxidase have unique features differentiating them from other amine oxidases. This review highlights the key attributes of the sarcosine oxidase family enzymes, in terms of their substrate binding motif, type of oxidation reaction mediated and FAD regeneration, to define the boundaries of this group and demarcate these enzymes from other amine oxidase families.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2021.108868</identifier><identifier>PMID: 33812916</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alkaloids ; Coenzyme reoxidation ; Covalent flavinylation ; d-amino acid oxidase family ; Demethylated products ; FAD ; Flavoenzymes ; Sarcosine oxidase family ; SOX motif</subject><ispartof>Archives of biochemistry and biophysics, 2021-06, Vol.704, p.108868-108868, Article 108868</ispartof><rights>2021 The Authors</rights><rights>Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396t-6bdd702073a4e2825fad94094fe84bbab70d1306b780b4b00e716273b9e2aaa53</citedby><cites>FETCH-LOGICAL-c396t-6bdd702073a4e2825fad94094fe84bbab70d1306b780b4b00e716273b9e2aaa53</cites><orcidid>0000-0002-3608-4029 ; 0000-0002-6421-3529</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2021.108868$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33812916$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lahham, Majd</creatorcontrib><creatorcontrib>Jha, Shalinee</creatorcontrib><creatorcontrib>Goj, Dominic</creatorcontrib><creatorcontrib>Macheroux, Peter</creatorcontrib><creatorcontrib>Wallner, Silvia</creatorcontrib><title>The family of sarcosine oxidases: Same reaction, different products</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subsequent spontaneous non-enzymatic reactions, forming an array of different products. These products range from demethylated simple species to complex alkaloids. The enzymes belonging to the sarcosine oxidase family, namely, monomeric and heterotetrameric sarcosine oxidase, l-pipecolate oxidase, N-methyltryptophan oxidase, NikD, l-proline dehydrogenase, FsqB, fructosamine oxidase and saccharopine oxidase have unique features differentiating them from other amine oxidases. This review highlights the key attributes of the sarcosine oxidase family enzymes, in terms of their substrate binding motif, type of oxidation reaction mediated and FAD regeneration, to define the boundaries of this group and demarcate these enzymes from other amine oxidase families.</description><subject>Alkaloids</subject><subject>Coenzyme reoxidation</subject><subject>Covalent flavinylation</subject><subject>d-amino acid oxidase family</subject><subject>Demethylated products</subject><subject>FAD</subject><subject>Flavoenzymes</subject><subject>Sarcosine oxidase family</subject><subject>SOX motif</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9kMtOwzAQRS0EoqXwAWxQlixIGdup48AKVbykSiwoa8uPiXCVB9gJon9PqhSWrEYjnXtHcwg5pzCnQMX1Zq6NmTNgdNilFPKATCkUIgUus0MyBQCeFlLQCTmJcQNAaSbYMZlwLikrqJiS5fodk1LXvtombZlEHWwbfYNJ--2djhhvklddYxJQ2863zVXifFliwKZLPkLretvFU3JU6iri2X7OyNvD_Xr5lK5eHp-Xd6vU8kJ0qTDO5cAg5zpDJtmi1K7IoMhKlJkx2uTgKAdhcgkmMwCYU8FybgpkWusFn5HLsXc4_Nlj7FTto8Wq0g22fVRsMUgodhUDSkfUhjbGgKX6CL7WYasoqJ07tVGDO7Vzp0Z3Q-ZiX9-bGt1f4lfWANyOAA5PfnkMKlqPjUXnA9pOudb_U_8DeAx90g</recordid><startdate>20210615</startdate><enddate>20210615</enddate><creator>Lahham, Majd</creator><creator>Jha, Shalinee</creator><creator>Goj, Dominic</creator><creator>Macheroux, Peter</creator><creator>Wallner, Silvia</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3608-4029</orcidid><orcidid>https://orcid.org/0000-0002-6421-3529</orcidid></search><sort><creationdate>20210615</creationdate><title>The family of sarcosine oxidases: Same reaction, different products</title><author>Lahham, Majd ; Jha, Shalinee ; Goj, Dominic ; Macheroux, Peter ; Wallner, Silvia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-6bdd702073a4e2825fad94094fe84bbab70d1306b780b4b00e716273b9e2aaa53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Alkaloids</topic><topic>Coenzyme reoxidation</topic><topic>Covalent flavinylation</topic><topic>d-amino acid oxidase family</topic><topic>Demethylated products</topic><topic>FAD</topic><topic>Flavoenzymes</topic><topic>Sarcosine oxidase family</topic><topic>SOX motif</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lahham, Majd</creatorcontrib><creatorcontrib>Jha, Shalinee</creatorcontrib><creatorcontrib>Goj, Dominic</creatorcontrib><creatorcontrib>Macheroux, Peter</creatorcontrib><creatorcontrib>Wallner, Silvia</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lahham, Majd</au><au>Jha, Shalinee</au><au>Goj, Dominic</au><au>Macheroux, Peter</au><au>Wallner, Silvia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The family of sarcosine oxidases: Same reaction, different products</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2021-06-15</date><risdate>2021</risdate><volume>704</volume><spage>108868</spage><epage>108868</epage><pages>108868-108868</pages><artnum>108868</artnum><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subsequent spontaneous non-enzymatic reactions, forming an array of different products. These products range from demethylated simple species to complex alkaloids. The enzymes belonging to the sarcosine oxidase family, namely, monomeric and heterotetrameric sarcosine oxidase, l-pipecolate oxidase, N-methyltryptophan oxidase, NikD, l-proline dehydrogenase, FsqB, fructosamine oxidase and saccharopine oxidase have unique features differentiating them from other amine oxidases. This review highlights the key attributes of the sarcosine oxidase family enzymes, in terms of their substrate binding motif, type of oxidation reaction mediated and FAD regeneration, to define the boundaries of this group and demarcate these enzymes from other amine oxidase families.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>33812916</pmid><doi>10.1016/j.abb.2021.108868</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-3608-4029</orcidid><orcidid>https://orcid.org/0000-0002-6421-3529</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0003-9861 |
ispartof | Archives of biochemistry and biophysics, 2021-06, Vol.704, p.108868-108868, Article 108868 |
issn | 0003-9861 1096-0384 |
language | eng |
recordid | cdi_proquest_miscellaneous_2508891306 |
source | ScienceDirect Journals (5 years ago - present) |
subjects | Alkaloids Coenzyme reoxidation Covalent flavinylation d-amino acid oxidase family Demethylated products FAD Flavoenzymes Sarcosine oxidase family SOX motif |
title | The family of sarcosine oxidases: Same reaction, different products |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T07%3A35%3A58IST&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=The%20family%20of%20sarcosine%20oxidases:%20Same%20reaction,%20different%20products&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Lahham,%20Majd&rft.date=2021-06-15&rft.volume=704&rft.spage=108868&rft.epage=108868&rft.pages=108868-108868&rft.artnum=108868&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/j.abb.2021.108868&rft_dat=%3Cproquest_cross%3E2508891306%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=2508891306&rft_id=info:pmid/33812916&rft_els_id=S0003986121001181&rfr_iscdi=true |