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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Archives of biochemistry and biophysics 2021-06, Vol.704, p.108868-108868, Article 108868
Hauptverfasser: Lahham, Majd, Jha, Shalinee, Goj, Dominic, Macheroux, Peter, Wallner, Silvia
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