Inactivation of β-lactamases from Enterobacter cloacae by monophosphams
Amongst the monocyclic β-lactam antibiotics, selected monophosphams were potent mechanism-based inactivators of the P99 and E2 cephalosporinases of Enterobacter cloacae. Inhibition of these enzymes was time-dependent with second order rate constants for inactivation of 100,000 to 20,000,000 1/mole/m...
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| Veröffentlicht in: | Journal of antimicrobial chemotherapy 1988-12, Vol.22 (6), p.801-809 |
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| container_end_page | 809 |
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| container_issue | 6 |
| container_start_page | 801 |
| container_title | Journal of antimicrobial chemotherapy |
| container_volume | 22 |
| creator | Bush, Karen Smith, S. A. Tanaka, S. K. Bonner, D. P. |
| description | Amongst the monocyclic β-lactam antibiotics, selected monophosphams were potent mechanism-based inactivators of the P99 and E2 cephalosporinases of Enterobacter cloacae. Inhibition of these enzymes was time-dependent with second order rate constants for inactivation of 100,000 to 20,000,000 1/mole/min. After incubation for 24 h at least 99% of the enzymatic activity was inhibited when enzyme was exposed to a ten-fold excess of inactivator. Amongst the monophosphams three classes of inhibitors were seen: irreversible inactivators as described above, transient inactivators and competitive (inhibitory) substrates. |
| doi_str_mv | 10.1093/jac/22.6.801 |
| format | Article |
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A. ; Tanaka, S. K. ; Bonner, D. P.</creator><creatorcontrib>Bush, Karen ; Smith, S. A. ; Tanaka, S. K. ; Bonner, D. P.</creatorcontrib><description>Amongst the monocyclic β-lactam antibiotics, selected monophosphams were potent mechanism-based inactivators of the P99 and E2 cephalosporinases of Enterobacter cloacae. Inhibition of these enzymes was time-dependent with second order rate constants for inactivation of 100,000 to 20,000,000 1/mole/min. After incubation for 24 h at least 99% of the enzymatic activity was inhibited when enzyme was exposed to a ten-fold excess of inactivator. Amongst the monophosphams three classes of inhibitors were seen: irreversible inactivators as described above, transient inactivators and competitive (inhibitory) substrates.</description><identifier>ISSN: 0305-7453</identifier><identifier>EISSN: 1460-2091</identifier><identifier>DOI: 10.1093/jac/22.6.801</identifier><identifier>PMID: 3266620</identifier><identifier>CODEN: JACHDX</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Anti-Bacterial Agents - pharmacology ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; beta-Lactamase Inhibitors ; beta-Lactamases - isolation & purification ; Biological and medical sciences ; Cephalosporinase - isolation & purification ; Enterobacter - enzymology ; Enterobacteriaceae - enzymology ; Medical sciences ; Microbial Sensitivity Tests ; Monobactams - pharmacology ; Organophosphorus Compounds - pharmacology ; Pharmacology. 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K.</creatorcontrib><creatorcontrib>Bonner, D. P.</creatorcontrib><title>Inactivation of β-lactamases from Enterobacter cloacae by monophosphams</title><title>Journal of antimicrobial chemotherapy</title><addtitle>J Antimicrob Chemother</addtitle><description>Amongst the monocyclic β-lactam antibiotics, selected monophosphams were potent mechanism-based inactivators of the P99 and E2 cephalosporinases of Enterobacter cloacae. Inhibition of these enzymes was time-dependent with second order rate constants for inactivation of 100,000 to 20,000,000 1/mole/min. After incubation for 24 h at least 99% of the enzymatic activity was inhibited when enzyme was exposed to a ten-fold excess of inactivator. Amongst the monophosphams three classes of inhibitors were seen: irreversible inactivators as described above, transient inactivators and competitive (inhibitory) substrates.</description><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>beta-Lactamase Inhibitors</subject><subject>beta-Lactamases - isolation & purification</subject><subject>Biological and medical sciences</subject><subject>Cephalosporinase - isolation & purification</subject><subject>Enterobacter - enzymology</subject><subject>Enterobacteriaceae - enzymology</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Monobactams - pharmacology</subject><subject>Organophosphorus Compounds - pharmacology</subject><subject>Pharmacology. 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P.</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</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>19881201</creationdate><title>Inactivation of β-lactamases from Enterobacter cloacae by monophosphams</title><author>Bush, Karen ; Smith, S. A. ; Tanaka, S. K. ; Bonner, D. P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-3af07e74fe042ca3ba3f16c2aa12c513f54eb13fcf062fd7ec167c58980e4be63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>beta-Lactamase Inhibitors</topic><topic>beta-Lactamases - isolation & purification</topic><topic>Biological and medical sciences</topic><topic>Cephalosporinase - isolation & purification</topic><topic>Enterobacter - enzymology</topic><topic>Enterobacteriaceae - enzymology</topic><topic>Medical sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Monobactams - pharmacology</topic><topic>Organophosphorus Compounds - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bush, Karen</creatorcontrib><creatorcontrib>Smith, S. A.</creatorcontrib><creatorcontrib>Tanaka, S. K.</creatorcontrib><creatorcontrib>Bonner, D. 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P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inactivation of β-lactamases from Enterobacter cloacae by monophosphams</atitle><jtitle>Journal of antimicrobial chemotherapy</jtitle><addtitle>J Antimicrob Chemother</addtitle><date>1988-12-01</date><risdate>1988</risdate><volume>22</volume><issue>6</issue><spage>801</spage><epage>809</epage><pages>801-809</pages><issn>0305-7453</issn><eissn>1460-2091</eissn><coden>JACHDX</coden><abstract>Amongst the monocyclic β-lactam antibiotics, selected monophosphams were potent mechanism-based inactivators of the P99 and E2 cephalosporinases of Enterobacter cloacae. Inhibition of these enzymes was time-dependent with second order rate constants for inactivation of 100,000 to 20,000,000 1/mole/min. After incubation for 24 h at least 99% of the enzymatic activity was inhibited when enzyme was exposed to a ten-fold excess of inactivator. 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| identifier | ISSN: 0305-7453 |
| ispartof | Journal of antimicrobial chemotherapy, 1988-12, Vol.22 (6), p.801-809 |
| issn | 0305-7453 1460-2091 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals Digital Archive Legacy |
| subjects | Anti-Bacterial Agents - pharmacology Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents beta-Lactamase Inhibitors beta-Lactamases - isolation & purification Biological and medical sciences Cephalosporinase - isolation & purification Enterobacter - enzymology Enterobacteriaceae - enzymology Medical sciences Microbial Sensitivity Tests Monobactams - pharmacology Organophosphorus Compounds - pharmacology Pharmacology. Drug treatments |
| title | Inactivation of β-lactamases from Enterobacter cloacae by monophosphams |
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