Search Results - "Mitić, Natasa"

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  1. 1

    Purple acid phosphatase: A journey into the function and mechanism of a colorful enzyme by Schenk, Gerhard, Mitić, Nataša, Hanson, Graeme R., Comba, Peter

    Published in Coordination chemistry reviews (15-01-2013)
    “…► Purple acid phosphatase (PAP) is a target for novel anti-osteoporotic drugs. ► PAP requires a mixed-valent metal center (Fe3+–M2+) for activity. ► PAP is…”
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  2. 2

    The Catalytic Mechanisms of Binuclear Metallohydrolases by Mitić, Nataša, Smith, Sarah J, Neves, Ademir, Guddat, Luke W, Gahan, Lawrence R, Schenk, Gerhard

    Published in Chemical reviews (01-08-2006)
    “…Binuclear metallohydrolases are a structurally diverse group of enzymes that use binuclear metal ion centers to catalyze the hydrolysis of amides and esters of…”
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  3. 3

    Binuclear Metallohydrolases: Complex Mechanistic Strategies for a Simple Chemical Reaction by Schenk, Gerhard, Mitić, Nataša, Gahan, Lawrence R, Ollis, David L, McGeary, Ross P, Guddat, Luke W

    Published in Accounts of chemical research (18-09-2012)
    “…Binuclear metallohydrolases are a large family of enzymes that require two closely spaced transition metal ions to carry out a plethora of hydrolytic…”
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  4. 4

    Human tartrate-resistant acid phosphatase becomes an effective ATPase upon proteolytic activation by Mitić, Nataša, Valizadeh, Mohsen, Leung, Eleanor W.W., de Jersey, John, Hamilton, Susan, Hume, David A., Cassady, A. Ian, Schenk, Gerhard

    Published in Archives of biochemistry and biophysics (15-07-2005)
    “…Proteolytic cleavage in an exposed loop of human tartrate-resistant acid phosphatase (TRAcP) with trypsin leads to a significant increase in activity. At each…”
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  5. 5

    Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks by Miraula, Manfredi, Schenk, Gerhard, Mitić, Nataša

    Published in Journal of inorganic biochemistry (01-09-2016)
    “…MIM-1 and MIM-2 are two recently identified metallo-β-lactamases (MBLs) from Novosphingobium pentaromativorans and Simiduia agarivorans, respectively. Since…”
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    The Divalent Metal Ion in the Active Site of Uteroferrin Modulates Substrate Binding and Catalysis by Mitić, Nataša, Hadler, Kieran S, Gahan, Lawrence R, Hengge, Alvan C, Schenk, Gerhard

    Published in Journal of the American Chemical Society (26-05-2010)
    “…The purple acid phosphatases (PAP) are binuclear metallohydrolases that catalyze the hydrolysis of a broad range of phosphomonoester substrates. The mode of…”
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  8. 8

    Organophosphate-degrading metallohydrolases: Structure and function of potent catalysts for applications in bioremediation by Schenk, Gerhard, Mateen, Irsa, Ng, Tee-Kheang, Pedroso, Marcelo M., Mitić, Nataša, Jafelicci, Miguel, Marques, Rodrigo F.C., Gahan, Lawrence R., Ollis, David L.

    Published in Coordination chemistry reviews (15-06-2016)
    “…•Organophosphate (OPs) compounds are heavily used pesticides in agriculture.•OPs are highly toxic and present a threat to human health and the environment.•A…”
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  9. 9

    Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops by Feder, Daniel, McGeary, Ross P., Mitić, Natasa, Lonhienne, Thierry, Furtado, Agnelo, Schulz, Benjamin L., Henry, Robert J., Schmidt, Susanne, Guddat, Luke W., Schenk, Gerhard

    Published in Plant science (Limerick) (01-05-2020)
    “…•Purple acid phosphatases (PAPs) play an important role in phosphate acquisition.•Plants possess PAPs with diverse substrate specificities (e.g.phytate,…”
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  10. 10

    Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms by Selleck, Christopher, Pedroso, Marcelo Monteiro, Wilson, Liam, Krco, Stefan, Knaven, Esmée Gianna, Miraula, Manfredi, Mitić, Nataša, Larrabee, James A., Brück, Thomas, Clark, Alice, Guddat, Luke W., Schenk, Gerhard

    Published in Scientific reports (30-07-2020)
    “…Genes that confer antibiotic resistance can rapidly be disseminated from one microorganism to another by mobile genetic elements, thus transferring resistance…”
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  11. 11

    Structural Flexibility Enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning Its Mechanism of Hydrolysis by Hadler, Kieran S, Mitić, Nataša, Ely, Fernanda, Hanson, Graeme R, Gahan, Lawrence R, Larrabee, James A, Ollis, David L, Schenk, Gerhard

    Published in Journal of the American Chemical Society (26-08-2009)
    “…The glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) belongs to the family of binuclear metallohydrolases and has attracted recent attention due to…”
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  12. 12

    Electronic Structure Analysis of the Dinuclear Metal Center in the Bioremediator Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes by Hadler, Kieran S, Mitić, Nataša, Yip, Sylvia Hsu-Chen, Gahan, Lawrence R, Ollis, David L, Schenk, Gerhard, Larrabee, James A

    Published in Inorganic chemistry (15-03-2010)
    “…The glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a promiscuous, dinuclear metallohydrolase that has potential application in the remediation…”
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  13. 13

    Insights into an evolutionary strategy leading to antibiotic resistance by Hou, Chun-Feng D., Liu, Jian-wei, Collyer, Charles, Mitić, Nataša, Pedroso, Marcelo Monteiro, Schenk, Gerhard, Ollis, David L.

    Published in Scientific reports (11-01-2017)
    “…Metallo-β-lactamases (MBLs) with activity towards a broad-spectrum of β-lactam antibiotics have become a major threat to public health, not least due to their…”
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  14. 14

    Spectroscopic and Electronic Structure Studies of Intermediate X in Ribonucleotide Reductase R2 and Two Variants:  A Description of the FeIV-Oxo Bond in the FeIII−O−FeIV Dimer by Mitić, Nataša, Clay, Michael D, Saleh, Lana, Bollinger, J. Martin, Solomon, Edward I

    Published in Journal of the American Chemical Society (25-07-2007)
    “…Spectroscopic and electronic structure studies of the class I Escherichia coli ribonucleotide reductase (RNR) intermediate X and three computationally derived…”
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  15. 15

    Mechanistic Insight from Calorimetric Measurements of the Assembly of the Binuclear Metal Active Site of Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes by Pedroso, Marcelo M, Ely, Fernanda, Carpenter, Margaret C, Mitić, Nataša, Gahan, Lawrence R, Ollis, David L, Wilcox, Dean E, Schenk, Gerhard

    Published in Biochemistry (Easton) (05-07-2017)
    “…Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a binuclear metallohydrolase with a high affinity for metal ions at its α site but a lower…”
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  16. 16

    X-ray Absorption Spectroscopic Investigation of the Resting Ferrous and Cosubstrate-Bound Active Sites of Phenylalanine Hydroxylase by Wasinger, Erik C, Mitić, Nataša, Hedman, Britt, Caradonna, John, Solomon, Edward I, Hodgson, Keith O

    Published in Biochemistry (Easton) (21-05-2002)
    “…Previous studies of ferrous wild-type phenylalanine hydroxylase, {Fe2+}PAHT[], have shown the active site to be a six-coordinate distorted octahedral site…”
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  17. 17

    Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme by Selleck, Christopher, Clayton, Daniel, Gahan, Lawrence R., Mitić, Nataša, McGeary, Ross P., Pedroso, Marcelo Monteiro, Guddat, Luke W., Schenk, Gerhard

    Published in Chemistry : a European journal (06-04-2017)
    “…Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for…”
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    β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health by Miraula, Manfredi, Whitaker, Jacob J., Schenk, Gerhard, Mitić, Nataša

    Published in Journal of biological inorganic chemistry (01-06-2015)
    “…Metallo-β-lactamases (MBLs) are a family of Zn(II)-dependent enzymes that inactivate most of the commonly used β-lactam antibiotics. They have emerged as a…”
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  20. 20

    CaII Binding Regulates and Dominates the Reactivity of a Transition-Metal-Ion-Dependent Diesterase from Mycobacterium tuberculosis by Pedroso, Marcelo M., Larrabee, James A., Ely, Fernanda, Gwee, Shuhui E., Mitić, Nataša, Ollis, David L., Gahan, Lawrence R., Schenk, Gerhard

    Published in Chemistry : a European journal (18-01-2016)
    “…The diesterase Rv0805 from Mycobacterium tuberculosis is a dinuclear metallohydrolase that plays an important role in signal transduction by controlling the…”
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