Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species
The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from race...
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| Veröffentlicht in: | Biochemistry (Easton) 1985-06, Vol.24 (12), p.2955-2958 |
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| container_issue | 12 |
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| container_title | Biochemistry (Easton) |
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| creator | Dix, Thomas A Bollag, Gideon E Domanico, Paul Benkovic, Stephen J |
| description | The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from racemic 6-methyltetrahydropterin requires stereoselectivity of the oxygenation. The absolute configuration of this new stereocenter is 4a(S)-hydroxy-6(RS)-methyltetrahydropterin by analogy to the CD spectrum of one of the four stereoisomers of 5-deaza-4a-hydroxy-6-methyltetrahydropterin. The source of the 4a-hydroxy oxygen is O2, as demonstrated by the observation of a 18O-induced 13C shift in the 13C NMR spectrum of the adduct when generated from [4a-13C]-6-methyltetrahydropterin and 18O2. |
| doi_str_mv | 10.1021/bi00333a022 |
| format | Article |
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As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from racemic 6-methyltetrahydropterin requires stereoselectivity of the oxygenation. The absolute configuration of this new stereocenter is 4a(S)-hydroxy-6(RS)-methyltetrahydropterin by analogy to the CD spectrum of one of the four stereoisomers of 5-deaza-4a-hydroxy-6-methyltetrahydropterin. The source of the 4a-hydroxy oxygen is O2, as demonstrated by the observation of a 18O-induced 13C shift in the 13C NMR spectrum of the adduct when generated from [4a-13C]-6-methyltetrahydropterin and 18O2.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00333a022</identifier><identifier>PMID: 4016080</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Biopterins - analogs & derivatives ; Biopterins - metabolism ; C.D ; Chromatography, High Pressure Liquid ; Circular Dichroism ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Gas Chromatography-Mass Spectrometry ; liver ; Liver - enzymology ; Magnetic Resonance Spectroscopy ; Optical Rotation ; Oxidoreductases ; phenylalanine 4-monooxygenase ; Phenylalanine Hydroxylase - metabolism ; Pteridines - metabolism ; Rats ; Spectrophotometry, Ultraviolet ; Stereoisomerism ; Structure-Activity Relationship</subject><ispartof>Biochemistry (Easton), 1985-06, Vol.24 (12), p.2955-2958</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a414t-dfb64d1947ce307f7697846938db6f654a3080dec6235bb8ab8d562accefba2c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00333a022$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00333a022$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27055,27903,27904,56717,56767</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8594884$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4016080$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dix, Thomas A</creatorcontrib><creatorcontrib>Bollag, Gideon E</creatorcontrib><creatorcontrib>Domanico, Paul</creatorcontrib><creatorcontrib>Benkovic, Stephen J</creatorcontrib><title>Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from racemic 6-methyltetrahydropterin requires stereoselectivity of the oxygenation. The absolute configuration of this new stereocenter is 4a(S)-hydroxy-6(RS)-methyltetrahydropterin by analogy to the CD spectrum of one of the four stereoisomers of 5-deaza-4a-hydroxy-6-methyltetrahydropterin. The source of the 4a-hydroxy oxygen is O2, as demonstrated by the observation of a 18O-induced 13C shift in the 13C NMR spectrum of the adduct when generated from [4a-13C]-6-methyltetrahydropterin and 18O2.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biopterins - analogs & derivatives</subject><subject>Biopterins - metabolism</subject><subject>C.D</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Circular Dichroism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Optical Rotation</subject><subject>Oxidoreductases</subject><subject>phenylalanine 4-monooxygenase</subject><subject>Phenylalanine Hydroxylase - metabolism</subject><subject>Pteridines - metabolism</subject><subject>Rats</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Stereoisomerism</subject><subject>Structure-Activity Relationship</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcGL1DAUxoMo6zh68izkIHqQatKkaepNFncVBhxwRPASXtLXnaydtCYt7Pz3Zp0yeBA85T2-Hx8v30fIc87eclbyd9YzJoQAVpYPyIpXJStk01QPyYoxpoqyUewxeZLSbV4lq-UFuZCMK6bZiozbPYZjDz0EH5Duj20c7vKe8D0Fm4Z-npC6IXT-Zo4w-SFQCC1Nwxwd0qGjmb7BcD9Ne6QSisViwinCn3mcMPpA04jOY3pKHnXQJ3y2vGvy7erj7vJTsfly_fnyw6YAyeVUtJ1VsuWNrB0KVne1amotVSN0a1WnKgki39-iU6WorNVgdVupEpzDzkLpxJq8OvmOcfg1Y5rMwSeHff4oDnMyteJNLQX_L8il0JLnhNfkzQl0cUgpYmfG6A8Qj4Yzc1-E-auITL9YbGd7wPbMLsln_eWiQ3LQdxGC8-mM6aqRWsuMFSfMpwnvzjLEn0bVoq7MbvvVbL5fiR-b653ZZv71iQeXzG1uKeSQ_3ngb_9Qrik</recordid><startdate>19850604</startdate><enddate>19850604</enddate><creator>Dix, Thomas A</creator><creator>Bollag, Gideon E</creator><creator>Domanico, Paul</creator><creator>Benkovic, Stephen J</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19850604</creationdate><title>Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species</title><author>Dix, Thomas A ; Bollag, Gideon E ; Domanico, Paul ; Benkovic, Stephen J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a414t-dfb64d1947ce307f7697846938db6f654a3080dec6235bb8ab8d562accefba2c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biopterins - analogs & derivatives</topic><topic>Biopterins - metabolism</topic><topic>C.D</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Circular Dichroism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>liver</topic><topic>Liver - enzymology</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Optical Rotation</topic><topic>Oxidoreductases</topic><topic>phenylalanine 4-monooxygenase</topic><topic>Phenylalanine Hydroxylase - metabolism</topic><topic>Pteridines - metabolism</topic><topic>Rats</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Stereoisomerism</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dix, Thomas A</creatorcontrib><creatorcontrib>Bollag, Gideon E</creatorcontrib><creatorcontrib>Domanico, Paul</creatorcontrib><creatorcontrib>Benkovic, Stephen J</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dix, Thomas A</au><au>Bollag, Gideon E</au><au>Domanico, Paul</au><au>Benkovic, Stephen J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1985-06-04</date><risdate>1985</risdate><volume>24</volume><issue>12</issue><spage>2955</spage><epage>2958</epage><pages>2955-2958</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from racemic 6-methyltetrahydropterin requires stereoselectivity of the oxygenation. The absolute configuration of this new stereocenter is 4a(S)-hydroxy-6(RS)-methyltetrahydropterin by analogy to the CD spectrum of one of the four stereoisomers of 5-deaza-4a-hydroxy-6-methyltetrahydropterin. The source of the 4a-hydroxy oxygen is O2, as demonstrated by the observation of a 18O-induced 13C shift in the 13C NMR spectrum of the adduct when generated from [4a-13C]-6-methyltetrahydropterin and 18O2.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>4016080</pmid><doi>10.1021/bi00333a022</doi><tpages>4</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1985-06, Vol.24 (12), p.2955-2958 |
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| language | eng |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Biopterins - analogs & derivatives Biopterins - metabolism C.D Chromatography, High Pressure Liquid Circular Dichroism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gas Chromatography-Mass Spectrometry liver Liver - enzymology Magnetic Resonance Spectroscopy Optical Rotation Oxidoreductases phenylalanine 4-monooxygenase Phenylalanine Hydroxylase - metabolism Pteridines - metabolism Rats Spectrophotometry, Ultraviolet Stereoisomerism Structure-Activity Relationship |
| title | Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species |
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