A general NMR method for the assay of racemase activity with optically active or optically inactive substrates
A rapid and sensitive method is described for determining the activity of alanine racemase (5.1.1.1) with its substrates. Alanine racemase from Bacillus subtilis catalyzes the exchange of the α hydrogen of l and d alanine, a racemic mixture of alanine as well as both the α hydrogens of glycine with...
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| Veröffentlicht in: | Analytical biochemistry 1975, Vol.63 (1), p.208-213 |
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| container_title | Analytical biochemistry |
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| creator | Babu, U.M. Johnston, R.B. McNeff, L.C. |
| description | A rapid and sensitive method is described for determining the activity of alanine racemase (5.1.1.1) with its substrates. Alanine racemase from
Bacillus subtilis catalyzes the exchange of the α hydrogen of
l and
d alanine, a racemic mixture of alanine as well as both the α hydrogens of glycine with D
2O. The rate of exchange which can be followed by NMR spectroscopy is proportional to the enzyme concentration. This assay has been used to test a wide variety of possible substrates and thus determine the specificity of the enzyme. |
| doi_str_mv | 10.1016/0003-2697(75)90206-7 |
| format | Article |
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Bacillus subtilis catalyzes the exchange of the α hydrogen of
l and
d alanine, a racemic mixture of alanine as well as both the α hydrogens of glycine with D
2O. The rate of exchange which can be followed by NMR spectroscopy is proportional to the enzyme concentration. This assay has been used to test a wide variety of possible substrates and thus determine the specificity of the enzyme.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(75)90206-7</identifier><identifier>PMID: 803321</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alanine - metabolism ; Bacillus subtilis - enzymology ; Deuterium ; Glycine - metabolism ; Isomerases - analysis ; Isomerases - metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Mathematics ; Optical Rotation ; Stereoisomerism</subject><ispartof>Analytical biochemistry, 1975, Vol.63 (1), p.208-213</ispartof><rights>1975</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-682289c370c94c7b7a2f06aa45ebd00b3ff08ffa77ee075ed3cfa57e62c639c63</citedby><cites>FETCH-LOGICAL-c356t-682289c370c94c7b7a2f06aa45ebd00b3ff08ffa77ee075ed3cfa57e62c639c63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003269775902067$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/803321$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Babu, U.M.</creatorcontrib><creatorcontrib>Johnston, R.B.</creatorcontrib><creatorcontrib>McNeff, L.C.</creatorcontrib><title>A general NMR method for the assay of racemase activity with optically active or optically inactive substrates</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>A rapid and sensitive method is described for determining the activity of alanine racemase (5.1.1.1) with its substrates. Alanine racemase from
Bacillus subtilis catalyzes the exchange of the α hydrogen of
l and
d alanine, a racemic mixture of alanine as well as both the α hydrogens of glycine with D
2O. The rate of exchange which can be followed by NMR spectroscopy is proportional to the enzyme concentration. This assay has been used to test a wide variety of possible substrates and thus determine the specificity of the enzyme.</description><subject>Alanine - metabolism</subject><subject>Bacillus subtilis - enzymology</subject><subject>Deuterium</subject><subject>Glycine - metabolism</subject><subject>Isomerases - analysis</subject><subject>Isomerases - metabolism</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mathematics</subject><subject>Optical Rotation</subject><subject>Stereoisomerism</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLJDEUhYP4ah__wEVWMrMovUmqkqqNIDLODPgA0XVIpW7sSD3aJK30v7faanTn4nLh3HMO3I-QEwZnDJg8BwCRcVmpX6r4XQEHmaktMmNQyQwEVNtk9mXZJwcxvgAwlhdyj-yWIARnM9Jf0mfsMZiW3t0-0A7TfGioGwJNc6QmRrOig6PBWOxMHBWb_JtPK_ru05wOi-StadvVpCMdc9-a7zdqXNYxBZMwHpEdZ9qIx5t9SJ6u_zxe_ctu7v_-v7q8yawoZMpkyXlZWaHAVrlVtTLcgTQmL7BuAGrhHJTOGaUQQRXYCOtMoVByK0U1ziE5nXoXYXhdYky689Fi25oeh2XUJVeciZyPxnwy2jDEGNDpRfCdCSvNQK8p6zVCvUaoVaE_KWs1xk42_cu6w-YrNGEdzxfTGccf3zwGHa3H3mLjA9qkm8H_3P8BJQSNVQ</recordid><startdate>1975</startdate><enddate>1975</enddate><creator>Babu, U.M.</creator><creator>Johnston, R.B.</creator><creator>McNeff, L.C.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>1975</creationdate><title>A general NMR method for the assay of racemase activity with optically active or optically inactive substrates</title><author>Babu, U.M. ; Johnston, R.B. ; McNeff, L.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-682289c370c94c7b7a2f06aa45ebd00b3ff08ffa77ee075ed3cfa57e62c639c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Alanine - metabolism</topic><topic>Bacillus subtilis - enzymology</topic><topic>Deuterium</topic><topic>Glycine - metabolism</topic><topic>Isomerases - analysis</topic><topic>Isomerases - metabolism</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mathematics</topic><topic>Optical Rotation</topic><topic>Stereoisomerism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Babu, U.M.</creatorcontrib><creatorcontrib>Johnston, R.B.</creatorcontrib><creatorcontrib>McNeff, L.C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Babu, U.M.</au><au>Johnston, R.B.</au><au>McNeff, L.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A general NMR method for the assay of racemase activity with optically active or optically inactive substrates</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1975</date><risdate>1975</risdate><volume>63</volume><issue>1</issue><spage>208</spage><epage>213</epage><pages>208-213</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>A rapid and sensitive method is described for determining the activity of alanine racemase (5.1.1.1) with its substrates. Alanine racemase from
Bacillus subtilis catalyzes the exchange of the α hydrogen of
l and
d alanine, a racemic mixture of alanine as well as both the α hydrogens of glycine with D
2O. The rate of exchange which can be followed by NMR spectroscopy is proportional to the enzyme concentration. This assay has been used to test a wide variety of possible substrates and thus determine the specificity of the enzyme.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>803321</pmid><doi>10.1016/0003-2697(75)90206-7</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2697 |
| ispartof | Analytical biochemistry, 1975, Vol.63 (1), p.208-213 |
| issn | 0003-2697 1096-0309 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82721342 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Alanine - metabolism Bacillus subtilis - enzymology Deuterium Glycine - metabolism Isomerases - analysis Isomerases - metabolism Kinetics Magnetic Resonance Spectroscopy Mathematics Optical Rotation Stereoisomerism |
| title | A general NMR method for the assay of racemase activity with optically active or optically inactive substrates |
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