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Journal Abstract Search

109 related items for PubMed ID: 24057071

  • 1. Zinc-selective inhibition of the promiscuous bacterial amide-hydrolase DapE: implications of metal heterogeneity for evolution and antibiotic drug design.
    Uda NR, Upert G, Angelici G, Nicolet S, Schmidt T, Schwede T, Creus M.
    Metallomics; 2014 Jan; 6(1):88-95. PubMed ID: 24057071
    [Abstract] [Full Text] [Related]

  • 2. Substrate specificity, metal binding properties, and spectroscopic characterization of the DapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae.
    Bienvenue DL, Gilner DM, Davis RS, Bennett B, Holz RC.
    Biochemistry; 2003 Sep 16; 42(36):10756-63. PubMed ID: 12962500
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  • 3. Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase.
    Usha V, Lloyd AJ, Roper DI, Dowson CG, Kozlov G, Gehring K, Chauhan S, Imam HT, Blindauer CA, Besra GS.
    Sci Rep; 2016 Mar 15; 6():23191. PubMed ID: 26976706
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  • 4. Inhibitors of bacterial N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) and demonstration of in vitro antimicrobial activity.
    Gillner D, Armoush N, Holz RC, Becker DP.
    Bioorg Med Chem Lett; 2009 Nov 15; 19(22):6350-2. PubMed ID: 19822427
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  • 6. Practical spectrophotometric assay for the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase, a potential antibiotic target.
    Heath TK, Lutz MR, Reidl CT, Guzman ER, Herbert CA, Nocek BP, Holz RC, Olsen KW, Ballicora MA, Becker DP.
    PLoS One; 2018 Nov 15; 13(4):e0196010. PubMed ID: 29698518
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  • 7. The structural and energetic aspects of substrate binding and the mechanism of action of the DapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) investigated using a hybrid QM/MM method.
    Dutta D, Mishra S.
    Phys Chem Chem Phys; 2014 Dec 21; 16(47):26348-58. PubMed ID: 25367594
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  • 9. Selectivity of Inhibition of N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase in Bacteria: The product of dapE-gene Is Not the Target of l-Captopril Antimicrobial Activity.
    Uda NR, Creus M.
    Bioinorg Chem Appl; 2011 Dec 21; 2011():306465. PubMed ID: 21577314
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  • 10. Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target.
    Gillner DM, Becker DP, Holz RC.
    J Biol Inorg Chem; 2013 Feb 21; 18(2):155-163. PubMed ID: 23223968
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  • 11. Hydrolysis of N-succinyl-L,L-diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: metal activation, solvent isotope effects, and kinetic mechanism.
    Born TL, Zheng R, Blanchard JS.
    Biochemistry; 1998 Jul 21; 37(29):10478-87. PubMed ID: 9671518
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  • 12. In silico approach towards identification of potential inhibitors of Helicobacter pylori DapE.
    Mandal RS, Das S.
    J Biomol Struct Dyn; 2015 Jul 21; 33(7):1460-73. PubMed ID: 25204745
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  • 14. The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues.
    Gillner DM, Bienvenue DL, Nocek BP, Joachimiak A, Zachary V, Bennett B, Holz RC.
    J Biol Inorg Chem; 2009 Jan 21; 14(1):1-10. PubMed ID: 18712420
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  • 16. Kinetic and spectroscopic characterization of the E134A- and E134D-altered dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae.
    Davis R, Bienvenue D, Swierczek SI, Gilner DM, Rajagopal L, Bennett B, Holz RC.
    J Biol Inorg Chem; 2006 Mar 21; 11(2):206-16. PubMed ID: 16421726
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  • 17. The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae is a dinuclear metallohydrolase.
    Cosper NJ, Bienvenue DL, Shokes JE, Gilner DM, Tsukamoto T, Scott RA, Holz RC.
    J Am Chem Soc; 2003 Dec 03; 125(48):14654-5. PubMed ID: 14640610
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  • 19. Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids.
    Terrazas-López M, Lobo-Galo N, Aguirre-Reyes LG, Cuen-Andrade JL, de la Rosa LA, Alvarez-Parrilla E, Martínez-Martínez A, Díaz-Sánchez ÁG.
    Biochimie; 2020 Oct 03; 177():198-212. PubMed ID: 32860896
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  • 20. The dimerization domain in DapE enzymes is required for catalysis.
    Nocek B, Starus A, Makowska-Grzyska M, Gutierrez B, Sanchez S, Jedrzejczak R, Mack JC, Olsen KW, Joachimiak A, Holz RC.
    PLoS One; 2014 Oct 03; 9(5):e93593. PubMed ID: 24806882
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