Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis
A selective screen for organisms that would metabolize o-phthalyl protected beta-lactams resulted in the discovery of a Xanthobacter agilis strain that contains an o-phthalyl amidase. The low level of enzyme expression in this organism could be enhanced by growing it on medium containing o-phthalate...
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| Veröffentlicht in: | Journal of molecular catalysis. B, Enzymatic Enzymatic, 1996-01, Vol.2 (1), p.53-69 |
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| container_title | Journal of molecular catalysis. B, Enzymatic |
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| creator | Briggs, Barbara S Kreuzman, Adam J Whitesitt, Celia Yeh, Wu-Kuang Zmijewski, Milton |
| description | A selective screen for organisms that would metabolize
o-phthalyl protected beta-lactams resulted in the discovery of a
Xanthobacter agilis strain that contains an
o-phthalyl amidase. The low level of enzyme expression in this organism could be enhanced by growing it on medium containing
o-phthalate. The enzyme was purified to near homogeneity by a 6-step procedure. The phthalyl amidase was characterized for its molecular mass, amino acid composition, internal sequences, catalytic and kinetic properties. No metal ion was required by or stimulatory to the enzyme. The amidase catalyzed conversion could be complete with a reaction stoichiometry of 1:1. The pH and temperature stability of the enzyme is improved significantly by increasing ionic strength of the buffer. The enzyme exhibits a broad substrate specificity for
o-phthalylated amides; however, it demonstrates an absolute requirement for the
o-phthalyl protecting group. The broad substrate acceptance, high catalytic activity, and stability at high salt or substrate concentration of the enzyme indicates that it can serve as a gentle method for deprotecting phthalimido and
o-phthalyl protected amides in new chemo-enzymatic synthetic routes. |
| doi_str_mv | 10.1016/1381-1177(96)00011-2 |
| format | Article |
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o-phthalyl protected beta-lactams resulted in the discovery of a
Xanthobacter agilis strain that contains an
o-phthalyl amidase. The low level of enzyme expression in this organism could be enhanced by growing it on medium containing
o-phthalate. The enzyme was purified to near homogeneity by a 6-step procedure. The phthalyl amidase was characterized for its molecular mass, amino acid composition, internal sequences, catalytic and kinetic properties. No metal ion was required by or stimulatory to the enzyme. The amidase catalyzed conversion could be complete with a reaction stoichiometry of 1:1. The pH and temperature stability of the enzyme is improved significantly by increasing ionic strength of the buffer. The enzyme exhibits a broad substrate specificity for
o-phthalylated amides; however, it demonstrates an absolute requirement for the
o-phthalyl protecting group. The broad substrate acceptance, high catalytic activity, and stability at high salt or substrate concentration of the enzyme indicates that it can serve as a gentle method for deprotecting phthalimido and
o-phthalyl protected amides in new chemo-enzymatic synthetic routes.</description><identifier>ISSN: 1381-1177</identifier><identifier>EISSN: 1873-3158</identifier><identifier>DOI: 10.1016/1381-1177(96)00011-2</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Characterization ; Enzyme discovery ; Fundamental and applied biological sciences. Psychology ; Miscellaneous ; Mission oriented research ; Purification ; Specificity</subject><ispartof>Journal of molecular catalysis. B, Enzymatic, 1996-01, Vol.2 (1), p.53-69</ispartof><rights>1996</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-eb3967d6091e5e423985e4d105172e8d743fd931930baf7574406ad99213ec13</citedby><cites>FETCH-LOGICAL-c400t-eb3967d6091e5e423985e4d105172e8d743fd931930baf7574406ad99213ec13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/1381-1177(96)00011-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3244106$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Briggs, Barbara S</creatorcontrib><creatorcontrib>Kreuzman, Adam J</creatorcontrib><creatorcontrib>Whitesitt, Celia</creatorcontrib><creatorcontrib>Yeh, Wu-Kuang</creatorcontrib><creatorcontrib>Zmijewski, Milton</creatorcontrib><title>Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis</title><title>Journal of molecular catalysis. B, Enzymatic</title><description>A selective screen for organisms that would metabolize
o-phthalyl protected beta-lactams resulted in the discovery of a
Xanthobacter agilis strain that contains an
o-phthalyl amidase. The low level of enzyme expression in this organism could be enhanced by growing it on medium containing
o-phthalate. The enzyme was purified to near homogeneity by a 6-step procedure. The phthalyl amidase was characterized for its molecular mass, amino acid composition, internal sequences, catalytic and kinetic properties. No metal ion was required by or stimulatory to the enzyme. The amidase catalyzed conversion could be complete with a reaction stoichiometry of 1:1. The pH and temperature stability of the enzyme is improved significantly by increasing ionic strength of the buffer. The enzyme exhibits a broad substrate specificity for
o-phthalylated amides; however, it demonstrates an absolute requirement for the
o-phthalyl protecting group. The broad substrate acceptance, high catalytic activity, and stability at high salt or substrate concentration of the enzyme indicates that it can serve as a gentle method for deprotecting phthalimido and
o-phthalyl protected amides in new chemo-enzymatic synthetic routes.</description><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Characterization</subject><subject>Enzyme discovery</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Miscellaneous</subject><subject>Mission oriented research</subject><subject>Purification</subject><subject>Specificity</subject><issn>1381-1177</issn><issn>1873-3158</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNp9kM1OwzAQhCMEElB4Aw4-IARSA944ieMLEiq_UiUuFeJmufaGGqVxsNNKfXscWjhy2j18M7szSXIG9BoolDfAKkgBOL8U5RWlFCDN9pIjqDhLGRTVftx_kcPkOITPCGUA1VHydm-Ddmv0mzHpVt7WVqveunZMVGtI512HvrcYiKuJS7tFv1DNpiFqaY0KSGrvluRdtf3CzZXu0RP1YRsbTpKDWjUBT3dzlMweH2aT53T6-vQyuZumOqe0T3HORMlNSQVggXnGRBWHAVoAz7AyPGe1EQwEo3NV84LnOS2VESIDhhrYKLnY2sZHv1YYermMcbBpVItuFWTMTqM6i2C-BbV3IXisZeftUvmNBCqHDuVQkBwKkqKUPx3KQXa-81dBq6b2qtU2_GlZludAy4jdbjGMUdcWvQzaYqvRWI-6l8bZ_-98A6vohGc</recordid><startdate>19960101</startdate><enddate>19960101</enddate><creator>Briggs, Barbara S</creator><creator>Kreuzman, Adam J</creator><creator>Whitesitt, Celia</creator><creator>Yeh, Wu-Kuang</creator><creator>Zmijewski, Milton</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>19960101</creationdate><title>Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis</title><author>Briggs, Barbara S ; Kreuzman, Adam J ; Whitesitt, Celia ; Yeh, Wu-Kuang ; Zmijewski, Milton</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-eb3967d6091e5e423985e4d105172e8d743fd931930baf7574406ad99213ec13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Characterization</topic><topic>Enzyme discovery</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Miscellaneous</topic><topic>Mission oriented research</topic><topic>Purification</topic><topic>Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Briggs, Barbara S</creatorcontrib><creatorcontrib>Kreuzman, Adam J</creatorcontrib><creatorcontrib>Whitesitt, Celia</creatorcontrib><creatorcontrib>Yeh, Wu-Kuang</creatorcontrib><creatorcontrib>Zmijewski, Milton</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of molecular catalysis. B, Enzymatic</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Briggs, Barbara S</au><au>Kreuzman, Adam J</au><au>Whitesitt, Celia</au><au>Yeh, Wu-Kuang</au><au>Zmijewski, Milton</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis</atitle><jtitle>Journal of molecular catalysis. B, Enzymatic</jtitle><date>1996-01-01</date><risdate>1996</risdate><volume>2</volume><issue>1</issue><spage>53</spage><epage>69</epage><pages>53-69</pages><issn>1381-1177</issn><eissn>1873-3158</eissn><abstract>A selective screen for organisms that would metabolize
o-phthalyl protected beta-lactams resulted in the discovery of a
Xanthobacter agilis strain that contains an
o-phthalyl amidase. The low level of enzyme expression in this organism could be enhanced by growing it on medium containing
o-phthalate. The enzyme was purified to near homogeneity by a 6-step procedure. The phthalyl amidase was characterized for its molecular mass, amino acid composition, internal sequences, catalytic and kinetic properties. No metal ion was required by or stimulatory to the enzyme. The amidase catalyzed conversion could be complete with a reaction stoichiometry of 1:1. The pH and temperature stability of the enzyme is improved significantly by increasing ionic strength of the buffer. The enzyme exhibits a broad substrate specificity for
o-phthalylated amides; however, it demonstrates an absolute requirement for the
o-phthalyl protecting group. The broad substrate acceptance, high catalytic activity, and stability at high salt or substrate concentration of the enzyme indicates that it can serve as a gentle method for deprotecting phthalimido and
o-phthalyl protected amides in new chemo-enzymatic synthetic routes.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/1381-1177(96)00011-2</doi><tpages>17</tpages></addata></record> |
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| identifier | ISSN: 1381-1177 |
| ispartof | Journal of molecular catalysis. B, Enzymatic, 1996-01, Vol.2 (1), p.53-69 |
| issn | 1381-1177 1873-3158 |
| language | eng |
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| source | Access via ScienceDirect (Elsevier) |
| subjects | Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Characterization Enzyme discovery Fundamental and applied biological sciences. Psychology Miscellaneous Mission oriented research Purification Specificity |
| title | Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis |
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