Enzymes and pathways of polyamine breakdown in microorganisms
The information currently available on the breakdown of spermidine and putrescine by microorganisms is reviewed. Two major metabolic routes have been described, one for the free bases via δ 1-pyrroline (4-aminobutyraldehyde), the other via N-acetyl derivatives. In both pathways oxidases or aminotran...
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Veröffentlicht in: | FEMS microbiology letters 1992-06, Vol.88 (3), p.249-262 |
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description | The information currently available on the breakdown of spermidine and putrescine by microorganisms is reviewed. Two major metabolic routes have been described, one for the free bases via δ
1-pyrroline (4-aminobutyraldehyde), the other via
N-acetyl derivatives. In both pathways oxidases or aminotransferases are the key enzymes in removing the nitrogen atoms. The two routes converge at 4-aminobutyrate, which is then metabolized via succinate. The degradation of putrescine in
Escherichia coli has been well characterized at both genetic and biochemical levels, but for other bacteria much less information is available. The C
3 moiety of spermidine is broken down via β-alanine, but the metabolism of this compound and its precursors is poorly understood. In yeasts, a catabolic route for spermidine and putrescine via
N-acetyl derivatives has been described in
Candida boidinii, and the evidence for its occurrence in other species is reviewed. Except for the terminal step of this pathway, the same group of enzymes can metabolize both the C
3 and C
4 moieties of spermidine. It is likely that other routes of polyamine catabolism also exist in both bacteria and yeasts. |
doi_str_mv | 10.1016/0378-1097(92)90806-Y |
format | Article |
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1-pyrroline (4-aminobutyraldehyde), the other via
N-acetyl derivatives. In both pathways oxidases or aminotransferases are the key enzymes in removing the nitrogen atoms. The two routes converge at 4-aminobutyrate, which is then metabolized via succinate. The degradation of putrescine in
Escherichia coli has been well characterized at both genetic and biochemical levels, but for other bacteria much less information is available. The C
3 moiety of spermidine is broken down via β-alanine, but the metabolism of this compound and its precursors is poorly understood. In yeasts, a catabolic route for spermidine and putrescine via
N-acetyl derivatives has been described in
Candida boidinii, and the evidence for its occurrence in other species is reviewed. Except for the terminal step of this pathway, the same group of enzymes can metabolize both the C
3 and C
4 moieties of spermidine. It is likely that other routes of polyamine catabolism also exist in both bacteria and yeasts.</description><identifier>ISSN: 0378-1097</identifier><identifier>ISSN: 0168-6445</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/0378-1097(92)90806-Y</identifier><identifier>PMID: 1515162</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acetylputrescine ; Acetylspermidine ; Escherichia coli - enzymology ; Escherichia coli - metabolism ; Polyamine ; Polyamines - metabolism ; Putrescine ; Spermidine ; Yeasts - enzymology ; Yeasts - metabolism</subject><ispartof>FEMS microbiology letters, 1992-06, Vol.88 (3), p.249-262</ispartof><rights>1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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/1515162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Large, Peter J.</creatorcontrib><title>Enzymes and pathways of polyamine breakdown in microorganisms</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Rev</addtitle><description>The information currently available on the breakdown of spermidine and putrescine by microorganisms is reviewed. Two major metabolic routes have been described, one for the free bases via δ
1-pyrroline (4-aminobutyraldehyde), the other via
N-acetyl derivatives. In both pathways oxidases or aminotransferases are the key enzymes in removing the nitrogen atoms. The two routes converge at 4-aminobutyrate, which is then metabolized via succinate. The degradation of putrescine in
Escherichia coli has been well characterized at both genetic and biochemical levels, but for other bacteria much less information is available. The C
3 moiety of spermidine is broken down via β-alanine, but the metabolism of this compound and its precursors is poorly understood. In yeasts, a catabolic route for spermidine and putrescine via
N-acetyl derivatives has been described in
Candida boidinii, and the evidence for its occurrence in other species is reviewed. Except for the terminal step of this pathway, the same group of enzymes can metabolize both the C
3 and C
4 moieties of spermidine. It is likely that other routes of polyamine catabolism also exist in both bacteria and yeasts.</description><subject>Acetylputrescine</subject><subject>Acetylspermidine</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - metabolism</subject><subject>Polyamine</subject><subject>Polyamines - metabolism</subject><subject>Putrescine</subject><subject>Spermidine</subject><subject>Yeasts - enzymology</subject><subject>Yeasts - metabolism</subject><issn>0378-1097</issn><issn>0168-6445</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtOwzAQRS0EKqXwByBlhWAR8CN2nAVIqCoPqRIbWHRlOc4YDIlT7JQqfD0prdAsZnGPrmYOQqcEXxFMxDVmuUwJLvKLgl4WWGKRLvbQmPA8S0Uh5D4a_yOH6CjGD4xxRrEYoRHhwwg6Rjcz_9M3EBPtq2Spu_e17mPS2mTZ1r1unIekDKA_q3btE-eTxpnQtuFNexebeIwOrK4jnOz2BL3ez16mj-n8-eFpejdPgeG8Sy3lVHIrpbFYZjZnWJSUQ2Etk0QKonNTUEkwAy650WVFuZElK6UklnCbsQk63_YuQ_u1gtipxkUDda09tKuockYEo0QO4NkOXJUNVGoZXKNDr3b_DvntNofh2m8HQUXjwBuoXADTqap1imC18as28tRGniqo-vOrFuwX6f1rmA</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>Large, Peter J.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19920601</creationdate><title>Enzymes and pathways of polyamine breakdown in microorganisms</title><author>Large, Peter J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e307t-f25285f88cf084f7306b25e9ff381861a7c928103e585cabd25c8b3b881f15f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Acetylputrescine</topic><topic>Acetylspermidine</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - metabolism</topic><topic>Polyamine</topic><topic>Polyamines - metabolism</topic><topic>Putrescine</topic><topic>Spermidine</topic><topic>Yeasts - enzymology</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Large, Peter J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Large, Peter J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymes and pathways of polyamine breakdown in microorganisms</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Rev</addtitle><date>1992-06-01</date><risdate>1992</risdate><volume>88</volume><issue>3</issue><spage>249</spage><epage>262</epage><pages>249-262</pages><issn>0378-1097</issn><issn>0168-6445</issn><eissn>1574-6968</eissn><abstract>The information currently available on the breakdown of spermidine and putrescine by microorganisms is reviewed. Two major metabolic routes have been described, one for the free bases via δ
1-pyrroline (4-aminobutyraldehyde), the other via
N-acetyl derivatives. In both pathways oxidases or aminotransferases are the key enzymes in removing the nitrogen atoms. The two routes converge at 4-aminobutyrate, which is then metabolized via succinate. The degradation of putrescine in
Escherichia coli has been well characterized at both genetic and biochemical levels, but for other bacteria much less information is available. The C
3 moiety of spermidine is broken down via β-alanine, but the metabolism of this compound and its precursors is poorly understood. In yeasts, a catabolic route for spermidine and putrescine via
N-acetyl derivatives has been described in
Candida boidinii, and the evidence for its occurrence in other species is reviewed. Except for the terminal step of this pathway, the same group of enzymes can metabolize both the C
3 and C
4 moieties of spermidine. It is likely that other routes of polyamine catabolism also exist in both bacteria and yeasts.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>1515162</pmid><doi>10.1016/0378-1097(92)90806-Y</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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source | Oxford Journals Open Access Collection; MEDLINE; Wiley Online Library Journals Frontfile Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Oxford University Press Journals Digital Archive Legacy |
subjects | Acetylputrescine Acetylspermidine Escherichia coli - enzymology Escherichia coli - metabolism Polyamine Polyamines - metabolism Putrescine Spermidine Yeasts - enzymology Yeasts - metabolism |
title | Enzymes and pathways of polyamine breakdown in microorganisms |
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