Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum
Guanidinobutyrase (guanidinobutyrate amidinohydrolase, EC. 3.5.3.7) catalyzing the third step of the arginine oxygenase pathway in Brevibacterium helvolum IFO 12073 (ATCC 11822) was purified to homogeneity and characterized. The enzyme had a molecular weight of 190,000 and was composed of four appar...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1992, Vol.56 (5), p.773-777 |
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| container_title | Bioscience, biotechnology, and biochemistry |
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| creator | Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan)) Shimizu, E Hirata, H Imada, K Katsumi, T Sawamura, S |
| description | Guanidinobutyrase (guanidinobutyrate amidinohydrolase, EC. 3.5.3.7) catalyzing the third step of the arginine oxygenase pathway in Brevibacterium helvolum IFO 12073 (ATCC 11822) was purified to homogeneity and characterized. The enzyme had a molecular weight of 190,000 and was composed of four apparently identical subunits with a molecular weight of 45,000. The E(1%) value at 280 nm of the enzyme protein was 2.4. The enzyme contained 0.5 mol of firmly bound Zn
2+
per mol of subunit. The enzyme was highly specific for 4-guanidinobutyrate, but had a weak activity toward L- and D-arginine. The Michaelis constant (K
m
) for 4-guanidinobutyrate was 2.9 mM. The optimum pH was 9.0. Strong mixed type inhibition was observed with thioglycolate and several other thiol compounds. These properties were compared with those of the enzyme of fluorescent Pseudomonas and discussed. |
| doi_str_mv | 10.1271/bbb.56.773 |
| format | Article |
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2+
per mol of subunit. The enzyme was highly specific for 4-guanidinobutyrate, but had a weak activity toward L- and D-arginine. The Michaelis constant (K
m
) for 4-guanidinobutyrate was 2.9 mM. The optimum pH was 9.0. Strong mixed type inhibition was observed with thioglycolate and several other thiol compounds. These properties were compared with those of the enzyme of fluorescent Pseudomonas and discussed.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.56.773</identifier><identifier>PMID: 27286206</identifier><language>eng</language><publisher>Tokyo: Taylor & Francis</publisher><subject>Analytical, structural and metabolic biochemistry ; ARGININA ; ARGININE ; Biological and medical sciences ; BREVIBACTERIUM ; Brevibacterium helvolum ; DEGRADACION ; DEGRADATION ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; HIDROLASAS ; HYDROLASE ; HYDROLASES</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1992, Vol.56 (5), p.773-777</ispartof><rights>Copyright 1992 Taylor and Francis Group LLC 1992</rights><rights>1993 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c539t-b3183a3974706ff8661953bf620e5e9e8f68627d038516d5ecf5273639d3af113</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4923523$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27286206$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan))</creatorcontrib><creatorcontrib>Shimizu, E</creatorcontrib><creatorcontrib>Hirata, H</creatorcontrib><creatorcontrib>Imada, K</creatorcontrib><creatorcontrib>Katsumi, T</creatorcontrib><creatorcontrib>Sawamura, S</creatorcontrib><title>Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Guanidinobutyrase (guanidinobutyrate amidinohydrolase, EC. 3.5.3.7) catalyzing the third step of the arginine oxygenase pathway in Brevibacterium helvolum IFO 12073 (ATCC 11822) was purified to homogeneity and characterized. The enzyme had a molecular weight of 190,000 and was composed of four apparently identical subunits with a molecular weight of 45,000. The E(1%) value at 280 nm of the enzyme protein was 2.4. The enzyme contained 0.5 mol of firmly bound Zn
2+
per mol of subunit. The enzyme was highly specific for 4-guanidinobutyrate, but had a weak activity toward L- and D-arginine. The Michaelis constant (K
m
) for 4-guanidinobutyrate was 2.9 mM. The optimum pH was 9.0. Strong mixed type inhibition was observed with thioglycolate and several other thiol compounds. These properties were compared with those of the enzyme of fluorescent Pseudomonas and discussed.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>ARGININA</subject><subject>ARGININE</subject><subject>Biological and medical sciences</subject><subject>BREVIBACTERIUM</subject><subject>Brevibacterium helvolum</subject><subject>DEGRADACION</subject><subject>DEGRADATION</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HIDROLASAS</subject><subject>HYDROLASE</subject><subject>HYDROLASES</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNp90c-L1DAUB_Agiju7evHoQQouIkLHpC8_mqMuOioDetBzeG2TMUubrEm7Mv-9GWZ2DyKeAuHzXt7Ll5BnjK5Zo9jbruvWQq6VggdkxYCrWmquHpIV1UzWLRfsjJznfE1puRDsMTlrVNPKhsoV2WwWDH7wIXbLvE-YbeViqrY1pp0PPthqsLuEA84-hsqH6n2yt77DfrbJL1P10463cVymJ-SRwzHbp6fzgvz4-OH71ad6-3Xz-erdtu4F6LnugLWAoBVXVDrXSsm0gM6VYayw2rZOlsHUQKEVTA7C9k40CiToAdAxBhfk9bHvTYq_FptnM_nc23HEYOOSDVNaypZrpQt99X8quabQHODLv-B1XFIoaxjGuQbNgUFRb46qTzHnZJ25SX7CtDeMmkMOpuRghDQlh4JfnFou3WSHe3r38QVcngDmHkeXMPQ-3zuuGxDNoY84Mh9KLBP-jmkczIz7Maa7Gvjn-8-PdQ6jwV0q7Ms3DRREq-EPVG6oTw</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan))</creator><creator>Shimizu, E</creator><creator>Hirata, H</creator><creator>Imada, K</creator><creator>Katsumi, T</creator><creator>Sawamura, S</creator><general>Taylor & Francis</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1992</creationdate><title>Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum</title><author>Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan)) ; Shimizu, E ; Hirata, H ; Imada, K ; Katsumi, T ; Sawamura, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c539t-b3183a3974706ff8661953bf620e5e9e8f68627d038516d5ecf5273639d3af113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>ARGININA</topic><topic>ARGININE</topic><topic>Biological and medical sciences</topic><topic>BREVIBACTERIUM</topic><topic>Brevibacterium helvolum</topic><topic>DEGRADACION</topic><topic>DEGRADATION</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HIDROLASAS</topic><topic>HYDROLASE</topic><topic>HYDROLASES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan))</creatorcontrib><creatorcontrib>Shimizu, E</creatorcontrib><creatorcontrib>Hirata, H</creatorcontrib><creatorcontrib>Imada, K</creatorcontrib><creatorcontrib>Katsumi, T</creatorcontrib><creatorcontrib>Sawamura, S</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yorifuji, T. (Shinshu Univ., Matsumoto, Nagano (Japan))</au><au>Shimizu, E</au><au>Hirata, H</au><au>Imada, K</au><au>Katsumi, T</au><au>Sawamura, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>1992</date><risdate>1992</risdate><volume>56</volume><issue>5</issue><spage>773</spage><epage>777</epage><pages>773-777</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Guanidinobutyrase (guanidinobutyrate amidinohydrolase, EC. 3.5.3.7) catalyzing the third step of the arginine oxygenase pathway in Brevibacterium helvolum IFO 12073 (ATCC 11822) was purified to homogeneity and characterized. The enzyme had a molecular weight of 190,000 and was composed of four apparently identical subunits with a molecular weight of 45,000. The E(1%) value at 280 nm of the enzyme protein was 2.4. The enzyme contained 0.5 mol of firmly bound Zn
2+
per mol of subunit. The enzyme was highly specific for 4-guanidinobutyrate, but had a weak activity toward L- and D-arginine. The Michaelis constant (K
m
) for 4-guanidinobutyrate was 2.9 mM. The optimum pH was 9.0. Strong mixed type inhibition was observed with thioglycolate and several other thiol compounds. These properties were compared with those of the enzyme of fluorescent Pseudomonas and discussed.</abstract><cop>Tokyo</cop><pub>Taylor & Francis</pub><pmid>27286206</pmid><doi>10.1271/bbb.56.773</doi><tpages>5</tpages></addata></record> |
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| source | J-STAGE Free; Freely Accessible Japanese Titles; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Analytical, structural and metabolic biochemistry ARGININA ARGININE Biological and medical sciences BREVIBACTERIUM Brevibacterium helvolum DEGRADACION DEGRADATION Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology HIDROLASAS HYDROLASE HYDROLASES |
| title | Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum |
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