Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization
ϵ-Poly- L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released L-lysine. The enzyme was a Co...
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| Veröffentlicht in: | FEMS microbiology letters 2002-02, Vol.207 (2), p.147-151 |
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| container_end_page | 151 |
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| container_issue | 2 |
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| container_title | FEMS microbiology letters |
| container_volume | 207 |
| creator | Kito, Mitsuaki Onji, Yuichi Yoshida, Toyokazu Nagasawa, Toru |
| description | ϵ-Poly-
L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain
Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released
L-lysine. The enzyme was a Co
2+ or Ca
2+ ion-activated aminopeptidase. |
| doi_str_mv | 10.1016/S0378-1097(01)00571-7 |
| format | Article |
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L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain
Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released
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L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain
Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released
L-lysine. The enzyme was a Co
2+ or Ca
2+ ion-activated aminopeptidase.</description><subject>Aminopeptidase</subject><subject>Aminopeptidases - chemistry</subject><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Flavobacterium - enzymology</subject><subject>Flavobacterium - isolation & purification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Polylysine - metabolism</subject><subject>Sphingobacterium multivorum</subject><subject>Substrate Specificity</subject><subject>ϵ-Poly- L-lysine</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0ktuFDEQBmALgcgkcASQN6CwMLjs7nY7G4QinhppFoG15Ud1YtQv7O5Ik2NwF87Bleh5ABskVi5Zn0p21U_IE-AvgUP16opLVTPgWp1zeMF5qYCpe2QFpSpYpav6Pln9ISfkNOevnPNC8OohOQHQZa2lWJHvG-_nlLD3SIeG_vzBxqHdMrpm7TbHHlnA62RD7K8p9nfbDmns_6GmocVk-4lejTeLHZz1E6Y4d7Sb2yneDmkpN5-AX9BxTrGJ3k5x6KntA_U3Nh343f7yEXnQ2Dbj4-N5Rr68e_v58gNbb95_vHyzZiiknpi2nFtX8iY4rEKluPIAaJ3QtQMQlW5Aci1rZ10QhYMQHNi6UCVYpYVU8ow8P_Qd0_BtxjyZLmaPbWt7HOZsFJRaVxL-C6EWqtaFWODTI5xdh8GMKXY2bc3vcS_g2RHY7G3bLCPzMf91hSilKHdPe31wuPz_NmIy2cfdjkJM6CcThmiAm10QzD4IZrdlw8Hsg2CU_AU_WqdY</recordid><startdate>20020205</startdate><enddate>20020205</enddate><creator>Kito, Mitsuaki</creator><creator>Onji, Yuichi</creator><creator>Yoshida, Toyokazu</creator><creator>Nagasawa, Toru</creator><general>Elsevier B.V</general><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20020205</creationdate><title>Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization</title><author>Kito, Mitsuaki ; Onji, Yuichi ; Yoshida, Toyokazu ; Nagasawa, Toru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e239t-9a00ab50fdbe6d6707c11eab298b11269f130938babd24b1ddb1a84751a792373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Aminopeptidase</topic><topic>Aminopeptidases - chemistry</topic><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Flavobacterium - enzymology</topic><topic>Flavobacterium - isolation & purification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Polylysine - metabolism</topic><topic>Sphingobacterium multivorum</topic><topic>Substrate Specificity</topic><topic>ϵ-Poly- L-lysine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kito, Mitsuaki</creatorcontrib><creatorcontrib>Onji, Yuichi</creatorcontrib><creatorcontrib>Yoshida, Toyokazu</creatorcontrib><creatorcontrib>Nagasawa, Toru</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kito, Mitsuaki</au><au>Onji, Yuichi</au><au>Yoshida, Toyokazu</au><au>Nagasawa, Toru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2002-02-05</date><risdate>2002</risdate><volume>207</volume><issue>2</issue><spage>147</spage><epage>151</epage><pages>147-151</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>ϵ-Poly-
L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain
Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released
L-lysine. The enzyme was a Co
2+ or Ca
2+ ion-activated aminopeptidase.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>11958932</pmid><doi>10.1016/S0378-1097(01)00571-7</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2002-02, Vol.207 (2), p.147-151 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71599631 |
| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Aminopeptidase Aminopeptidases - chemistry Aminopeptidases - isolation & purification Aminopeptidases - metabolism Bacteriology Biological and medical sciences Flavobacterium - enzymology Flavobacterium - isolation & purification Fundamental and applied biological sciences. Psychology Metabolism. Enzymes Microbiology Molecular Weight Polylysine - metabolism Sphingobacterium multivorum Substrate Specificity ϵ-Poly- L-lysine |
| title | Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization |
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