Search Results - "Mitić, Natasa"
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Purple acid phosphatase: A journey into the function and mechanism of a colorful enzyme
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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The Catalytic Mechanisms of Binuclear Metallohydrolases
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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Binuclear Metallohydrolases: Complex Mechanistic Strategies for a Simple Chemical Reaction
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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Human tartrate-resistant acid phosphatase becomes an effective ATPase upon proteolytic activation
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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Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks
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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Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse
Published in Protein & cell (01-08-2020)Get full text
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The Divalent Metal Ion in the Active Site of Uteroferrin Modulates Substrate Binding and Catalysis
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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Organophosphate-degrading metallohydrolases: Structure and function of potent catalysts for applications in bioremediation
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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Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops
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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Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms
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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Structural Flexibility Enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning Its Mechanism of Hydrolysis
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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Electronic Structure Analysis of the Dinuclear Metal Center in the Bioremediator Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes
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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Insights into an evolutionary strategy leading to antibiotic resistance
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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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
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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Mechanistic Insight from Calorimetric Measurements of the Assembly of the Binuclear Metal Active Site of Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes
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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X-ray Absorption Spectroscopic Investigation of the Resting Ferrous and Cosubstrate-Bound Active Sites of Phenylalanine Hydroxylase
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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Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme
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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Copper Ions and Coordination Complexes as Novel Carbapenem Adjuvants
Published in Antimicrobial agents and chemotherapy (01-02-2018)“…Carbapenem-resistant are urgent threats to global human health. These organisms produce β-lactamases with carbapenemase activity, such as the…”
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β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health
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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CaII Binding Regulates and Dominates the Reactivity of a Transition-Metal-Ion-Dependent Diesterase from Mycobacterium tuberculosis
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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