Inhibition of plant and microbial ureases by phosphoroamides
Enzyme kinetic studies of inhibition of plant (jackbean) and microbial (Bacillus pasteurii) ureases by eight phosphoroamides [phenylphosphorodiamidate, 4-chlorophenylphosphorodiamidate, phosphoric triamide, N-(diaminophosphinyl) benzamide, N-(diaminophosphinyl) benzeneacetamide, 4-chloro-N-(diaminop...
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| Veröffentlicht in: | Plant and soil 1990-10, Vol.127 (2), p.269-283 |
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| creator | McCarty, G.W. (Iowa State Univ., Ames, IA (USA). Dept. of Agronomy) Bremner, J.M Lee, J.S |
| description | Enzyme kinetic studies of inhibition of plant (jackbean) and microbial (Bacillus pasteurii) ureases by eight phosphoroamides [phenylphosphorodiamidate, 4-chlorophenylphosphorodiamidate, phosphoric triamide, N-(diaminophosphinyl) benzamide, N-(diaminophosphinyl) benzeneacetamide, 4-chloro-N-(diaminophosphinyl) benzamide, N-(4-nitrophenyl) phosphoric triamide, N-(diaminophosphinyl)-3-pyridinecarboxamide] demonstrated that these compounds are slow, tight-binding inhibitors of urease enzymes. Measurement of the dissociation constants (Ki*) of the enzyme-inhibitor complexes (E . I*) formed by interaction of the ureases and phosphoroamide inhibitors studied showed that these inhibitors had a much higher affinity (i. e., a lower Ki*) for plant urease than for microbial urease. Measurement of rate constants for formation (kon) and decay (koff) of E · I* showed that, whereas k on varied greatly with the different inhibitors and ureases, k off was constant for the phosphoroamides tested and had a characteristic value for each urease. The half-life of E · I* (30°C; pH 7 THAM buffer) for the plant urease was much longer than that for the microbial urease, and this difference largely accounted for the much higher values of Ki* (koff/kon) observed with microbial urease. |
| doi_str_mv | 10.1007/BF00014435 |
| format | Article |
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(Iowa State Univ., Ames, IA (USA). Dept. of Agronomy) ; Bremner, J.M ; Lee, J.S</creator><creatorcontrib>McCarty, G.W. (Iowa State Univ., Ames, IA (USA). Dept. of Agronomy) ; Bremner, J.M ; Lee, J.S</creatorcontrib><description>Enzyme kinetic studies of inhibition of plant (jackbean) and microbial (Bacillus pasteurii) ureases by eight phosphoroamides [phenylphosphorodiamidate, 4-chlorophenylphosphorodiamidate, phosphoric triamide, N-(diaminophosphinyl) benzamide, N-(diaminophosphinyl) benzeneacetamide, 4-chloro-N-(diaminophosphinyl) benzamide, N-(4-nitrophenyl) phosphoric triamide, N-(diaminophosphinyl)-3-pyridinecarboxamide] demonstrated that these compounds are slow, tight-binding inhibitors of urease enzymes. Measurement of the dissociation constants (Ki*) of the enzyme-inhibitor complexes (E . I*) formed by interaction of the ureases and phosphoroamide inhibitors studied showed that these inhibitors had a much higher affinity (i. e., a lower Ki*) for plant urease than for microbial urease. Measurement of rate constants for formation (kon) and decay (koff) of E · I* showed that, whereas k on varied greatly with the different inhibitors and ureases, k off was constant for the phosphoroamides tested and had a characteristic value for each urease. The half-life of E · I* (30°C; pH 7 THAM buffer) for the plant urease was much longer than that for the microbial urease, and this difference largely accounted for the much higher values of Ki* (koff/kon) observed with microbial urease.</description><identifier>ISSN: 0032-079X</identifier><identifier>EISSN: 1573-5036</identifier><identifier>DOI: 10.1007/BF00014435</identifier><identifier>CODEN: PLSOA2</identifier><language>eng</language><publisher>Dordrecht: Kluwer Academic Publishers</publisher><subject>Active sites ; Agricultural soils ; Agronomy. Soil science and plant productions ; AMIDAS ; AMIDE ; AMIDES ; Analytical estimating ; BACILLUS ; Biological and medical sciences ; CANAVALIA ENSIFORMIS ; Economic plant physiology ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Hydrolysis ; INHIBIDORES DE LA UREASA ; INHIBITEUR DE L'UREASE ; Kinetics ; Nutrition. Photosynthesis. Respiration. Metabolism ; phosphoroamides ; Soil biochemistry ; urease ; UREASE INHIBITORS ; Velocity</subject><ispartof>Plant and soil, 1990-10, Vol.127 (2), p.269-283</ispartof><rights>1990 Kluwer Academic Publishers</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c331t-69e48a5b4304324c3f0e88b1493b9063972a34aa456728a817e345a431cb933</citedby><cites>FETCH-LOGICAL-c331t-69e48a5b4304324c3f0e88b1493b9063972a34aa456728a817e345a431cb933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/42938653$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/42938653$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,778,782,801,27911,27912,58004,58237</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19354606$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>McCarty, G.W. (Iowa State Univ., Ames, IA (USA). Dept. of Agronomy)</creatorcontrib><creatorcontrib>Bremner, J.M</creatorcontrib><creatorcontrib>Lee, J.S</creatorcontrib><title>Inhibition of plant and microbial ureases by phosphoroamides</title><title>Plant and soil</title><description>Enzyme kinetic studies of inhibition of plant (jackbean) and microbial (Bacillus pasteurii) ureases by eight phosphoroamides [phenylphosphorodiamidate, 4-chlorophenylphosphorodiamidate, phosphoric triamide, N-(diaminophosphinyl) benzamide, N-(diaminophosphinyl) benzeneacetamide, 4-chloro-N-(diaminophosphinyl) benzamide, N-(4-nitrophenyl) phosphoric triamide, N-(diaminophosphinyl)-3-pyridinecarboxamide] demonstrated that these compounds are slow, tight-binding inhibitors of urease enzymes. Measurement of the dissociation constants (Ki*) of the enzyme-inhibitor complexes (E . I*) formed by interaction of the ureases and phosphoroamide inhibitors studied showed that these inhibitors had a much higher affinity (i. e., a lower Ki*) for plant urease than for microbial urease. Measurement of rate constants for formation (kon) and decay (koff) of E · I* showed that, whereas k on varied greatly with the different inhibitors and ureases, k off was constant for the phosphoroamides tested and had a characteristic value for each urease. The half-life of E · I* (30°C; pH 7 THAM buffer) for the plant urease was much longer than that for the microbial urease, and this difference largely accounted for the much higher values of Ki* (koff/kon) observed with microbial urease.</description><subject>Active sites</subject><subject>Agricultural soils</subject><subject>Agronomy. Soil science and plant productions</subject><subject>AMIDAS</subject><subject>AMIDE</subject><subject>AMIDES</subject><subject>Analytical estimating</subject><subject>BACILLUS</subject><subject>Biological and medical sciences</subject><subject>CANAVALIA ENSIFORMIS</subject><subject>Economic plant physiology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolysis</subject><subject>INHIBIDORES DE LA UREASA</subject><subject>INHIBITEUR DE L'UREASE</subject><subject>Kinetics</subject><subject>Nutrition. Photosynthesis. Respiration. Metabolism</subject><subject>phosphoroamides</subject><subject>Soil biochemistry</subject><subject>urease</subject><subject>UREASE INHIBITORS</subject><subject>Velocity</subject><issn>0032-079X</issn><issn>1573-5036</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNpFkEFLw0AQhRdRsFYvHgUhFz0I0dmd3SQLXrRYLRQ96MFbmKQbuyXJ1t300H9vSoo9DMPw3jw-HmOXHO45QPrwPAUALiWqIzbiKsVYASbHbASAIoZUf5-ysxBWsLt5MmKPs3ZpC9tZ10auitY1tV1E7SJqbOldYamONt5QMCEqttF66UI_3lFjFyacs5OK6mAu9nvMPqcvX5O3eP7xOps8zeMSkXdxoo3MSBUSQaKQJVZgsqzgUmOhIUGdCkJJJFWSiowynhqUiiTystCIY3Y7pK69-92Y0OWNDaWpe1TjNiHnKuOai7Q33g3GnjwEb6p87W1DfptzyHf15Id6evPNPpVCSXXlqS1tOHxoVDLp4cbsevCtQuf8vy6FxixRO7qrQa_I5fTj-4z3ueYgRF_xH2jOc-E</recordid><startdate>19901001</startdate><enddate>19901001</enddate><creator>McCarty, G.W. (Iowa State Univ., Ames, IA (USA). 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Soil science and plant productions</topic><topic>AMIDAS</topic><topic>AMIDE</topic><topic>AMIDES</topic><topic>Analytical estimating</topic><topic>BACILLUS</topic><topic>Biological and medical sciences</topic><topic>CANAVALIA ENSIFORMIS</topic><topic>Economic plant physiology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolysis</topic><topic>INHIBIDORES DE LA UREASA</topic><topic>INHIBITEUR DE L'UREASE</topic><topic>Kinetics</topic><topic>Nutrition. Photosynthesis. Respiration. Metabolism</topic><topic>phosphoroamides</topic><topic>Soil biochemistry</topic><topic>urease</topic><topic>UREASE INHIBITORS</topic><topic>Velocity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McCarty, G.W. (Iowa State Univ., Ames, IA (USA). Dept. of Agronomy)</creatorcontrib><creatorcontrib>Bremner, J.M</creatorcontrib><creatorcontrib>Lee, J.S</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Plant and soil</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McCarty, G.W. (Iowa State Univ., Ames, IA (USA). Dept. of Agronomy)</au><au>Bremner, J.M</au><au>Lee, J.S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of plant and microbial ureases by phosphoroamides</atitle><jtitle>Plant and soil</jtitle><date>1990-10-01</date><risdate>1990</risdate><volume>127</volume><issue>2</issue><spage>269</spage><epage>283</epage><pages>269-283</pages><issn>0032-079X</issn><eissn>1573-5036</eissn><coden>PLSOA2</coden><abstract>Enzyme kinetic studies of inhibition of plant (jackbean) and microbial (Bacillus pasteurii) ureases by eight phosphoroamides [phenylphosphorodiamidate, 4-chlorophenylphosphorodiamidate, phosphoric triamide, N-(diaminophosphinyl) benzamide, N-(diaminophosphinyl) benzeneacetamide, 4-chloro-N-(diaminophosphinyl) benzamide, N-(4-nitrophenyl) phosphoric triamide, N-(diaminophosphinyl)-3-pyridinecarboxamide] demonstrated that these compounds are slow, tight-binding inhibitors of urease enzymes. Measurement of the dissociation constants (Ki*) of the enzyme-inhibitor complexes (E . I*) formed by interaction of the ureases and phosphoroamide inhibitors studied showed that these inhibitors had a much higher affinity (i. e., a lower Ki*) for plant urease than for microbial urease. Measurement of rate constants for formation (kon) and decay (koff) of E · I* showed that, whereas k on varied greatly with the different inhibitors and ureases, k off was constant for the phosphoroamides tested and had a characteristic value for each urease. The half-life of E · I* (30°C; pH 7 THAM buffer) for the plant urease was much longer than that for the microbial urease, and this difference largely accounted for the much higher values of Ki* (koff/kon) observed with microbial urease.</abstract><cop>Dordrecht</cop><pub>Kluwer Academic Publishers</pub><doi>10.1007/BF00014435</doi><tpages>15</tpages></addata></record> |
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| ispartof | Plant and soil, 1990-10, Vol.127 (2), p.269-283 |
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| source | Jstor Complete Legacy; Springer Nature - Complete Springer Journals |
| subjects | Active sites Agricultural soils Agronomy. Soil science and plant productions AMIDAS AMIDE AMIDES Analytical estimating BACILLUS Biological and medical sciences CANAVALIA ENSIFORMIS Economic plant physiology Enzymes Fundamental and applied biological sciences. Psychology Hydrolysis INHIBIDORES DE LA UREASA INHIBITEUR DE L'UREASE Kinetics Nutrition. Photosynthesis. Respiration. Metabolism phosphoroamides Soil biochemistry urease UREASE INHIBITORS Velocity |
| title | Inhibition of plant and microbial ureases by phosphoroamides |
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