Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties
The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Re...
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| Veröffentlicht in: | Amino acids 2009, Vol.36 (1), p.99-106 |
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| creator | Austin, Christopher J. D Astelbauer, Florian Kosim-Satyaputra, Priambudi Ball, Helen J Willows, Robert D Jamie, Joanne F Hunt, Nicholas H |
| description | The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the α-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next. |
| doi_str_mv | 10.1007/s00726-008-0037-6 |
| format | Article |
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D ; Astelbauer, Florian ; Kosim-Satyaputra, Priambudi ; Ball, Helen J ; Willows, Robert D ; Jamie, Joanne F ; Hunt, Nicholas H</creator><creatorcontrib>Austin, Christopher J. D ; Astelbauer, Florian ; Kosim-Satyaputra, Priambudi ; Ball, Helen J ; Willows, Robert D ; Jamie, Joanne F ; Hunt, Nicholas H</creatorcontrib><description>The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the α-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-008-0037-6</identifier><identifier>PMID: 18274832</identifier><language>eng</language><publisher>Vienna: Vienna : Springer Vienna</publisher><subject>Amino Acid Sequence ; Amino acids ; Analytical Chemistry ; Animals ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Circular Dichroism ; Conversion ; Diseases ; Enzyme Stability ; Enzymes ; Human ; Humans ; Hydrogen-Ion Concentration ; Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry ; Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics ; Indoleamine-Pyrrole 2,3,-Dioxygenase - isolation & purification ; Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism ; Inhibitors ; Kinetics ; Kynurenine - chemistry ; Kynurenine - metabolism ; Life Sciences ; Mice ; Molecular Sequence Data ; Neurobiology ; Original Article ; Protein Folding ; Protein Structure, Secondary ; Proteins ; Proteomics ; Recombinant ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Alignment ; Studies ; Temperature</subject><ispartof>Amino acids, 2009, Vol.36 (1), p.99-106</ispartof><rights>Springer-Verlag 2008</rights><rights>Springer-Verlag 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-304211f17aa38a233e69520f4d99fed83ff311589e2704125aedb45acecf9ec3</citedby><cites>FETCH-LOGICAL-c458t-304211f17aa38a233e69520f4d99fed83ff311589e2704125aedb45acecf9ec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-008-0037-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-008-0037-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,4025,27928,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18274832$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Austin, Christopher J. D</creatorcontrib><creatorcontrib>Astelbauer, Florian</creatorcontrib><creatorcontrib>Kosim-Satyaputra, Priambudi</creatorcontrib><creatorcontrib>Ball, Helen J</creatorcontrib><creatorcontrib>Willows, Robert D</creatorcontrib><creatorcontrib>Jamie, Joanne F</creatorcontrib><creatorcontrib>Hunt, Nicholas H</creatorcontrib><title>Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the α-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Circular Dichroism</subject><subject>Conversion</subject><subject>Diseases</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Human</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry</subject><subject>Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics</subject><subject>Indoleamine-Pyrrole 2,3,-Dioxygenase - isolation & purification</subject><subject>Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism</subject><subject>Inhibitors</subject><subject>Kinetics</subject><subject>Kynurenine - chemistry</subject><subject>Kynurenine - metabolism</subject><subject>Life Sciences</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Recombinant</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Studies</subject><subject>Temperature</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkU-LFDEQxYMo7rj6AbxogyAebE1S6XRyXBb_wYoH13PIpCuzWbqTMekG59ub2R5QBPWQhCK_94qqR8hTRt8wSvu3pV5ctpSqeqBv5T2yYQJUy5nW98mGatCtEB07I49KuaWUccXkQ3LGFO-FAr4hu89pKdjYODQ3y2RjE-KQRrRTiNjw19AOIf047DDaSg2h7Ed7aEqa7oo5RDc325DcDU7B2fHOp8x5cfOSa7nPaY95DlgekwfejgWfnN5zcv3-3fXlx_bqy4dPlxdXrROdmluggjPmWW8tKMsBUOqOUy8GrT0OCrwHxjqlkfdUMN5ZHLaisw6d1-jgnLxcbWvn7wuW2UyhOBxHG7EOaqRUtAMN_wVBUg5KiAq--ifIZF-3CrqnFX3xB3qblhzruIZR3cleSH6k2Eq5nErJ6M0-h8nmQ4XMMVazxmpqrOYYq5FV8-zkvGwnHH4pTjlWgK9AqV9xh_n31n93fb6KvE3G7nIo5ttXThnQuuHKaPgJG5G2EA</recordid><startdate>2009</startdate><enddate>2009</enddate><creator>Austin, Christopher J. 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D</au><au>Astelbauer, Florian</au><au>Kosim-Satyaputra, Priambudi</au><au>Ball, Helen J</au><au>Willows, Robert D</au><au>Jamie, Joanne F</au><au>Hunt, Nicholas H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2009</date><risdate>2009</risdate><volume>36</volume><issue>1</issue><spage>99</spage><epage>106</epage><pages>99-106</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the α-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next.</abstract><cop>Vienna</cop><pub>Vienna : Springer Vienna</pub><pmid>18274832</pmid><doi>10.1007/s00726-008-0037-6</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Analytical Chemistry Animals Biochemical Engineering Biochemistry Biomedical and Life Sciences Circular Dichroism Conversion Diseases Enzyme Stability Enzymes Human Humans Hydrogen-Ion Concentration Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics Indoleamine-Pyrrole 2,3,-Dioxygenase - isolation & purification Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism Inhibitors Kinetics Kynurenine - chemistry Kynurenine - metabolism Life Sciences Mice Molecular Sequence Data Neurobiology Original Article Protein Folding Protein Structure, Secondary Proteins Proteomics Recombinant Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Alignment Studies Temperature |
| title | Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties |
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