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Stereospecificity of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme) [swine]
The stereospecificity of peptidyl dipeptide hydrolase [EC 3.4.15.1] was investigated. Six free and N-blocked alanyl peptides containing D-alanine were synthesized and tested as substrates. Their susceptibilities were determined by measuring Ala-Ala release by cation exchange column chromatography. T...
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Published in: | Journal of biochemistry (Tokyo) 1979-12, Vol.86 (6), p.1719-1724 |
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container_end_page | 1724 |
container_issue | 6 |
container_start_page | 1719 |
container_title | Journal of biochemistry (Tokyo) |
container_volume | 86 |
creator | OSHIMA, Genichiro NAGASAWA, Kinzo |
description | The stereospecificity of peptidyl dipeptide hydrolase [EC 3.4.15.1] was investigated. Six free and N-blocked alanyl peptides containing D-alanine were synthesized and tested as substrates. Their susceptibilities were determined by measuring Ala-Ala release by cation exchange column chromatography. Their Michaelis constants, Km values, and velocity maxima, Vmax values, were also determined. The enzyme showed high stereospecificity for an amino acyl residue in position 3 from C-terminus: it had an absolute requirement for the alanyl residue of the L-configuration in this position. An alanyl residue of the L-configuration in position 1 or 2 increased, but was not essential for activity. The enzyme showed little stereospecificity for an alanyl residue in position 4 from the C-terminus. |
doi_str_mv | 10.1093/oxfordjournals.jbchem.a132692 |
format | article |
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School of Pharmaceutical Sciences</creatorcontrib><description>The stereospecificity of peptidyl dipeptide hydrolase [EC 3.4.15.1] was investigated. Six free and N-blocked alanyl peptides containing D-alanine were synthesized and tested as substrates. Their susceptibilities were determined by measuring Ala-Ala release by cation exchange column chromatography. Their Michaelis constants, Km values, and velocity maxima, Vmax values, were also determined. The enzyme showed high stereospecificity for an amino acyl residue in position 3 from C-terminus: it had an absolute requirement for the alanyl residue of the L-configuration in this position. An alanyl residue of the L-configuration in position 1 or 2 increased, but was not essential for activity. The enzyme showed little stereospecificity for an alanyl residue in position 4 from the C-terminus.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a132692</identifier><identifier>PMID: 231034</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Kidney - enzymology ; Kinetics ; Peptidyl-Dipeptidase A - metabolism ; Protein Binding ; Stereoisomerism ; Substrate Specificity ; Swine</subject><ispartof>Journal of biochemistry (Tokyo), 1979-12, Vol.86 (6), p.1719-1724</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-fd6180ad95f364b6e32c2288953724988bc2ab190f46eb926e00c10089294a8e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27898,27899</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/231034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OSHIMA, Genichiro</creatorcontrib><creatorcontrib>NAGASAWA, Kinzo</creatorcontrib><creatorcontrib>Natsionalen Agrarno-Promishlen S"yuz, Sofia (Bulgaria)</creatorcontrib><creatorcontrib>Kitasato Univ., Tokyo (Japan). School of Pharmaceutical Sciences</creatorcontrib><title>Stereospecificity of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme) [swine]</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The stereospecificity of peptidyl dipeptide hydrolase [EC 3.4.15.1] was investigated. Six free and N-blocked alanyl peptides containing D-alanine were synthesized and tested as substrates. Their susceptibilities were determined by measuring Ala-Ala release by cation exchange column chromatography. Their Michaelis constants, Km values, and velocity maxima, Vmax values, were also determined. The enzyme showed high stereospecificity for an amino acyl residue in position 3 from C-terminus: it had an absolute requirement for the alanyl residue of the L-configuration in this position. An alanyl residue of the L-configuration in position 1 or 2 increased, but was not essential for activity. The enzyme showed little stereospecificity for an alanyl residue in position 4 from the C-terminus.</description><subject>Animals</subject><subject>Kidney - enzymology</subject><subject>Kinetics</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>Protein Binding</subject><subject>Stereoisomerism</subject><subject>Substrate Specificity</subject><subject>Swine</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><recordid>eNpVkFtv1DAQhS3EbSn8A4TyAoKHLL7FsR94qNrSdlUuEotUUSHLcSZbbxM72Flo-PWkyqoSTzOjc87M6EPoNcFLghV7H26bEOtt2EVv2rTcVvYauqUhjApFH6AFKQuRU1GQh2iBMSW5ovzyKXqW0vZupIw9QY8pI5jxBbr6NkCEkHqwrnHWDWMWmqyHfnD12Ga1m1vIrsc6htYkyN4e-o0LA_jkfHae2-B_Qxyc32Tg_44dvMuu0h_n4edz9KiZPoQX-3qAvn88WR-d5RdfTs-PDi9yy7ka8qYWRGJTq6JhglcCGLWUSqkKVlKupKwsNRVRuOECKkUFYGwJxlJRxY0EdoDezHv7GH7tIA26c8lC2xoPYZd0yacQlngyfpiNNoaUIjS6j64zcdQE6zu2-n-2emar92yn_Mv9oV3VQX2fnmFOcj7LLg1we6-aeKNFycpCn13-0J_Kz6er49Varyf_q9nfmKDNJrqkV1-JkhgXnKhSsn_Vb5aQ</recordid><startdate>197912</startdate><enddate>197912</enddate><creator>OSHIMA, Genichiro</creator><creator>NAGASAWA, Kinzo</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>7X8</scope></search><sort><creationdate>197912</creationdate><title>Stereospecificity of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme) [swine]</title><author>OSHIMA, Genichiro ; NAGASAWA, Kinzo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c449t-fd6180ad95f364b6e32c2288953724988bc2ab190f46eb926e00c10089294a8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Animals</topic><topic>Kidney - enzymology</topic><topic>Kinetics</topic><topic>Peptidyl-Dipeptidase A - metabolism</topic><topic>Protein Binding</topic><topic>Stereoisomerism</topic><topic>Substrate Specificity</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OSHIMA, Genichiro</creatorcontrib><creatorcontrib>NAGASAWA, Kinzo</creatorcontrib><creatorcontrib>Natsionalen Agrarno-Promishlen S"yuz, Sofia (Bulgaria)</creatorcontrib><creatorcontrib>Kitasato Univ., Tokyo (Japan). School of Pharmaceutical Sciences</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OSHIMA, Genichiro</au><au>NAGASAWA, Kinzo</au><aucorp>Natsionalen Agrarno-Promishlen S"yuz, Sofia (Bulgaria)</aucorp><aucorp>Kitasato Univ., Tokyo (Japan). School of Pharmaceutical Sciences</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stereospecificity of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme) [swine]</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1979-12</date><risdate>1979</risdate><volume>86</volume><issue>6</issue><spage>1719</spage><epage>1724</epage><pages>1719-1724</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>The stereospecificity of peptidyl dipeptide hydrolase [EC 3.4.15.1] was investigated. Six free and N-blocked alanyl peptides containing D-alanine were synthesized and tested as substrates. Their susceptibilities were determined by measuring Ala-Ala release by cation exchange column chromatography. Their Michaelis constants, Km values, and velocity maxima, Vmax values, were also determined. The enzyme showed high stereospecificity for an amino acyl residue in position 3 from C-terminus: it had an absolute requirement for the alanyl residue of the L-configuration in this position. An alanyl residue of the L-configuration in position 1 or 2 increased, but was not essential for activity. The enzyme showed little stereospecificity for an alanyl residue in position 4 from the C-terminus.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>231034</pmid><doi>10.1093/oxfordjournals.jbchem.a132692</doi><tpages>6</tpages></addata></record> |
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source | J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - English; Oxford University Press:Jisc Collections:Oxford Journal Archive: Access period 2024-2025 |
subjects | Animals Kidney - enzymology Kinetics Peptidyl-Dipeptidase A - metabolism Protein Binding Stereoisomerism Substrate Specificity Swine |
title | Stereospecificity of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme) [swine] |
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