user

N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-β-lactamase

被引：92
|
作者：
Siemann, S
Evanoff, DP
Marrone, L
Clarke, AJ
Viswanatha, T
Dmitrienko, GI
机构：
[1] Univ Waterloo, Dept Chem, Waterloo, ON N2L 3G1, Canada
[2] Univ Guelph, Dept Microbiol, Canadian Bacterial Dis Network, Guelph, ON N1G 2W1, Canada
来源：
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2002年 / 46卷 / 08期
关键词：
D O I：
10.1128/AAC.46.8.2450-2457.2002
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Members of a family of N-arylsulfonyl hydrazones have been identified as novel inhibitors of IMP-1, a metallo-beta-lactamase of increasing prevalence. Structure-activity relationship studies have indicated a requirement for bulky aromatic substituents on each side of the sulfonyl hydrazone backbone for these compounds to serve as efficient inhibitors of IMP-1. Molecular modeling has provided insight into the structural basis for the anti-metallo-beta-lactamase activity exhibited by this class of compounds.
引用
收藏
页码：2450 / 2457
页数：8
相关论文
共 50 条
  • [1] Appearance of IMP-1 metallo-β-lactamase in Europe
    Cornaglia, G
    Riccio, ML
    Mazzariol, A
    Lauretti, L
    Fontana, R
    Rossolini, GM
    LANCET, 1999, 353 (9156): : 899 - 900
  • [2] Synthesis and sar of thioester and thiol inhibitors of IMP-1 metallo-β-lactamase
    Greenlee, ML
    Laub, JB
    Balkovec, JM
    Hammond, ML
    Hammond, GG
    Pompliano, DL
    Epstein-Toney, JH
    BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 1999, 9 (17) : 2549 - 2554
  • [3] Structural and Kinetic Studies on Metallo-β-lactamase IMP-1
    Griffin, Dionne H.
    Richmond, Timothy K.
    Sanchez, Carlo
    Moller, Abraham Jon
    Breece, Robert M.
    Tierney, David L.
    Bennett, Brian
    Crowder, Michael W.
    BIOCHEMISTRY, 2011, 50 (42) : 9125 - 9134
  • [4] Spectroscopic and Biochemical Studies on Metallo-β-lactamase IMP-1
    Zhang, Huan
    FASEB JOURNAL, 2020, 34
  • [5] Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1
    Moloughney, JG
    Thomas, JD
    Toney, JH
    FEMS MICROBIOLOGY LETTERS, 2005, 243 (01) : 65 - 71
  • [6] Amino acid substitutions in a variant of IMP-1 metallo-β-lactamase
    Iyobe, S
    Kusadokoro, H
    Ozaki, J
    Matsumura, N
    Minami, S
    Haruta, S
    Sawai, T
    O'Hara, K
    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2000, 44 (08) : 2023 - 2027
  • [7] RNA-hydrolyzing activity of metallo-β-lactamase IMP-1
    Kato, Yoshiki
    Takahashi, Masayuki
    Seki, Mineaki
    Nashimoto, Masayuki
    Shimizu-Ibuka, Akiko
    PLOS ONE, 2020, 15 (10):
  • [8] Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-β-lactamase
    Toney, JH
    Hammond, GG
    Fitzgerald, PMD
    Sharma, N
    Balkovec, JM
    Rouen, GP
    Olson, SH
    Hammond, ML
    Greenlee, ML
    Gao, YD
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (34) : 31913 - 31918
  • [9] Triazolylthioacetamides Confer Inhibitory Efficacy against Metallo-β-Lactamase IMP-1
    Zhang, Yue-Juan
    Zhai, Le
    Wan, Yi
    Yang, Ke-Wu
    LETTERS IN DRUG DESIGN & DISCOVERY, 2021, 18 (01) : 76 - 84
  • [10] Insight into the mechanism of the IMP-1 metallo-β-lactamase by molecular dynamics simulations
    Oelschlaeger, P
    Schmid, RD
    Pleiss, J
    PROTEIN ENGINEERING, 2003, 16 (05): : 341 - 350
12345