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Genomes and Genes | Gerhard SchenkSummaryAffiliation: University of Queensland Country: Australia Publications
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Binuclear metallohydrolases: complex mechanistic strategies for a simple chemical reactionGerhard Schenk
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia
Acc Chem Res 45:1593-603. 2012..Here we only focus on catalytic strategies applied by the former group...
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphataseGerhard Schenk
Department of Biochemistry and Molecular Biology, School of Molecular and Microbial Sciences, University of Queensland, Brisbane 4072, Australia
Proc Natl Acad Sci U S A 102:273-8. 2005..The structure and kinetics support the hypothesis that the bridging oxygen atom initiates hydrolysis...- Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimeticsGerhard Schenk
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, QLD, 4072, Australia
J Biol Inorg Chem 13:139-55. 2008.... - Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycleGerhard Schenk
School of Molecular and Microbial Sciences, The University of Queensland, St, Lucia, QLD 4072, Australia
BMC Struct Biol 8:6. 2008..However, despite considerable effort in the last 10 years various aspects of the basic molecular mechanism of action are still not fully understood... 
Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenesKieran S Hadler
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, Queensland 4072, Australia
J Am Chem Soc 130:14129-38. 2008..Thus, it is proposed that GpdQ employs an intricate regulatory mechanism for catalysis, where coordination flexibility in one of the two metal binding sites is essential for optimal activity...- Phosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacterFernanda Ely
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia
J Inorg Biochem 106:19-22. 2012..Thus, similar to the binuclear metallohydrolases urease and purple acid phosphatase the tripodal arrangement of PO(4) is interpreted in terms of a role of the μOH as a reaction nucleophile... - Spectroscopic and catalytic characterization of a functional Fe(III)Fe(II) biomimetic for the active site of uteroferrin and protein cleavageSarah J Smith
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane 4072, Australia
Inorg Chem 51:2065-78. 2012..It is interesting to note that aqueous solutions of [Fe(III)Fe(II)L1(μ-OAc)(2)](+) are also capable of protein cleavage, at mild temperature and pH conditions, thus further expanding the scope of this complex's catalytic promiscuity... - The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysisNatasa Mitic
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia
J Am Chem Soc 132:7049-54. 2010.... - The reaction mechanism of the Ga(III)Zn(II) derivative of uteroferrin and corresponding biomimeticsSarah J Smith
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, QLD, Australia
J Biol Inorg Chem 12:1207-20. 2007.... - The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysisFernanda Ely
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD 4072, Australia
Biochem J 432:565-73. 2010..The observed mechanistic flexibility may reconcile contrasting reaction models that have been published previously and may be beneficial for the rapid adaptation of OP-degrading enzymes to changing environmental pressures... - Human tartrate-resistant acid phosphatase becomes an effective ATPase upon proteolytic activationNatasa Mitic
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, Australia
Arch Biochem Biophys 439:154-64. 2005..Notably, at low pH this residue may act as a proton donor for the leaving group. In this respect the mechanism of cleaved TRAcP resembles that of sweet potato purple acid phosphatase... - Electronic structure analysis of the dinuclear metal center in the bioremediator glycerophosphodiesterase (GpdQ) from Enterobacter aerogenesKieran S Hadler
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia
Inorg Chem 49:2727-34. 2010..This is the first study to investigate the electronic structure of an enzyme with a mu-1,1-carboxylate bridged dicobalt(II) center... - Structural and catalytic characterization of a heterovalent Mn(II)Mn(III) complex that mimics purple acid phosphatasesSarah J Smith
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane 4072, Australia
Inorg Chem 48:10036-48. 2009..2) is detected. Mechanistic implications are discussed... - The bioremediator glycerophosphodiesterase employs a non-processive mechanism for hydrolysisKieran S Hadler
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland 4072, Australia
J Inorg Biochem 104:211-3. 2010..Furthermore, the data indicate that the diester bonds are cleaved in two separate (non-processive) reactions, indicating that only a single nucleophile (the terminal hydroxide molecule) is likely to be employed as a nucleophile for GpdQ... - Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysisKieran S Hadler
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia
J Am Chem Soc 131:11900-8. 2009..Overall, the mechanism employed by GpdQ is a paradigm of a substrate- and metal-ion-induced fit to optimize catalysis... - Penicillin inhibitors of purple acid phosphatase- Faridoon
The University of Queensland, School of Chemistry and Molecular Biosciences, Brisbane, QLD 4072, Australia
Bioorg Med Chem Lett 22:2555-9. 2012..Molecular modelling has been used to examine the binding modes of these compounds in the active site of the enzyme and to rationalise their activities... - Electronic and geometric structures of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA)Fernanda Ely
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Australia
J Biol Inorg Chem 16:777-87. 2011..Mechanistic implications of these observations are discussed... - Metal-ion mutagenesis: conversion of a purple acid phosphatase from sweet potato to a neutral phosphatase with the formation of an unprecedented catalytically competent Mn(II)Mn(II) active siteNatasa Mitic
School of Chemistry and Molecular Biosciences, University of Queensland, Queensland, Australia, 4072
J Am Chem Soc 131:8173-9. 2009.... - The identification of new metallo-β-lactamase inhibitor leads from fragment-based screeningPeter Vella
The University of Queensland, School of Chemistry and Molecular Biosciences, Brisbane, QLD 4072, Australia
Bioorg Med Chem Lett 21:3282-5. 2011..The interactions between identified inhibitory fragments and the active site of the MBL from Klebsiella pneumoniae and Pseudomonas aeruginosa were probed by in silico docking studies... - Cadmium(II) complexes of the glycerophosphodiester-degrading enzyme GpdQ and a biomimetic N,O ligandRuth E Mirams
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, QLD, 4072, Australia
J Biol Inorg Chem 13:1065-72. 2008..9, with k(cat) = 0.004 s(-1). In summary, the model is both an adequate structural and a reasonable functional mimic of GpdQ... - The role of Zn-OR and Zn-OH nucleophiles and the influence of para-substituents in the reactions of binuclear phosphatase mimeticsLena J Daumann
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia
Dalton Trans 41:1695-708. 2012..The results are discussed with respect to the potential nucleophilic species (coordinated deprotonated alcohol versus coordinated hydroxide)... - Phosphotyrosyl peptides and analogues as substrates and inhibitors of purple acid phosphatasesMohsen Valizadeh
Department of Biochemistry, The University of Queensland, St. Lucia, QLD 4072, Australia
Arch Biochem Biophys 424:154-62. 2004..These compounds are thus the most potent organic inhibitors yet reported for the purple acid phosphatases... - Synthesis, modelling and kinetic assays of potent inhibitors of purple acid phosphataseSiti Hajar Mohd-Pahmi
The University of Queensland, School of Chemistry and Molecular Biosciences, Brisbane, QLD 4072, Australia
Bioorg Med Chem Lett 21:3092-4. 2011.... - 3-mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-β-lactamase inhibitors- Faridoon
The University of Queensland, School of Chemistry and Molecular Biosciences, Brisbane, QLD 4072, Australia
Bioorg Med Chem Lett 22:380-6. 2012..The interactions of these inhibitors with the active site of IMP-1 were examined using in silico methods... - Cadmium(II) complexes: mimics of organophosphate pesticide degrading enzymes and metallo-β-lactamasesLena J Daumann
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia
Inorg Chem 51:7669-81. 2012.... - Structural and spectroscopic studies of a model for catechol oxidaseSarah J Smith
School of Molecular and Microbial Sciences, The University of Queensland, St Lucia, QLD 4072, Australia
J Biol Inorg Chem 13:499-510. 2008..The complex also displays catecholase activity (k(cat) = 15 +/- 1.5 min(-1), K(M) = 6.4 +/- 1.8 mM), which is compared with other dicopper catechol oxidase models... - Direct electrochemistry of porcine purple acid phosphatase (uteroferrin)Paul V Bernhardt
Center for Metals in Biology, Department of Chemistry, University of Queensland, Brisbane 4072, Australia
Biochemistry 43:10387-92. 2004..The effect of pH on the redox potentials has been investigated in the range 3 < pH < 6.5, enabling acid dissociation constants for Uf(o) and its phosphate and arsenate complexes to be calculated... - Promiscuity comes at a price: Catalytic versatility vs efficiency in different metal ion derivatives of the potential bioremediator GpdQLena J Daumann
School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD 4072, Australia
Biochim Biophys Acta 1834:425-32. 2013..This article is part of a Special Issue entitled: Chemistry and mechanism of phosphatases, diesterases and triesterases... - Inhibition of purple acid phosphatase with alpha-alkoxynaphthylmethylphosphonic acidsRoss P McGeary
The University of Queensland, School of Molecular and Microbial Sciences, Brisbane, QLD, Australia
Bioorg Med Chem Lett 19:163-6. 2009..This manuscript describes the design and synthesis of derivatives of 1-naphthylmethylphosphonic acids as inhibitors of PAP. The K(i) values of these compounds are as low as 4 microM, the lowest reported to date for a PAP inhibitor... - The catalytic mechanisms of binuclear metallohydrolasesNatasa Mitic
School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, QLD 4072, Australia
Chem Rev 106:3338-63. 2006 - Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?Kieran S Hadler
School of Molecular and Microbial Sciences, The University of Queensland, St, Lucia, 4072, Australia
BMC Res Notes 1:78. 2008..Due to its role in bone resorption the 35 kDa TRAcP has become a promising target for the development of anti-osteoporotic chemotherapeutics... - Identification of purple acid phosphatase inhibitors by fragment-based screening: promising new leads for osteoporosis therapeuticsDaniel Feder
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia
Chem Biol Drug Des 80:665-74. 2012..These studies open the way to the design of more potent and selective inhibitors of purple acid phosphatases that can be tested as anti-osteoporotic drug leads... - Bacterial and Plant Ketol-Acid Reductoisomerases Have Different Mechanisms of Induced Fit during the Catalytic CycleSze Ho Wong
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia Electronic address
J Mol Biol 424:168-79. 2012..Support is thereby provided for the idea that plant and bacterial KARIs have evolved different mechanisms of induced fit to prepare the active site for catalysis... - Improving a Natural Enzyme Activity through Incorporation of Unnatural Amino AcidsIsaac N Ugwumba
Commonwealth Scientific and Industrial Research Organization, Black Mountain, Canberra, Australia, Research School of Chemistry, Australian National University, Canberra, Australia, School of Chemistry, University of Wollongong, Australia, School of Chemistry and Molecular Biosciences, University of Queensland, Australia, Department of Chemistry, National University of Ireland Maynooth, Ireland
J Am Chem Soc 133:326-33. 2011..These results demonstrate that designer amino acids provide easy access to new and valuable sequence and functional space for the engineering and evolution of existing enzyme functions... - Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preferenceColin J Jackson
Research School of Chemistry, Australian National University, Australia
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:681-5. 2008..Catalytic implications of the structure and its Fe2+ metal-ion preference are discussed... - A new heterobinuclear FeIIICuII complex with a single terminal FeIII-O(phenolate) bond. Relevance to purple acid phosphatases and nucleasesMauricio Lanznaster
, , Universidade Federal de Santa Catarina, Campus Trindade, , SC, Brazil
J Biol Inorg Chem 10:319-32. 2005..5 microM), under physiological conditions (optimum pH of 7.0), with a rate enhancement of 2.7 x 10(7) over the uncatalyzed reaction. Thus, 1 is one of the most effective model complexes to date, mimicking the function of nucleases... - Diesterase activity and substrate binding in purple acid phosphatasesRobynn S Cox
Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322-0300, USA
J Am Chem Soc 129:9550-1. 2007 - Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active siteColin J Jackson
Research School of Chemistry, Building 35, Australian National University, Canberra, ACT 0200, Australia
Biochem J 397:501-8. 2006..These results suggest an essential role for iron in the catalytic mechanism of bacterial phosphotriesterases, and that these phosphotriesterases are natively heterobinuclear iron-zinc enzymes... - Kinetic and spectroscopic studies of N694C lipoxygenase: a probe of the substrate activation mechanism of a nonheme ferric enzymeMichael L Neidig
Department of Chemistry, Stanford University, Stanford, California 94305, USA
J Am Chem Soc 129:7531-7. 2007.... - Reactivity of M(II) metal-substituted derivatives of pig purple acid phosphatase (uteroferrin) with phosphateMark B Twitchett
Department of Chemistry, University of Newcastle, Newcastle upon Tyne NE1 7RU, U.K
Inorg Chem 41:5787-94. 2002..8 and independent of M(II) (Fe(II), Zn(II), Mn(II)). The acid dissociation process is assigned to Fe(III)-OH(2) to Fe(III)-OH(-), where OH(-) is less readily displaced by phosphate... - Rapid-freeze-quench magnetic circular dichroism of intermediate X in ribonucleotide reductase: new structural insightNatasa Mitic
Department of Chemistry, Stanford University, 333 Campus Street, Stanford, California 94305, USA
J Am Chem Soc 125:11200-1. 2003.... - Using directed evolution to improve the solubility of the C-terminal domain of Escherichia coli aminopeptidase P. Implications for metal binding and protein stabilityJian Wei Liu
Research School of Chemistry, Australian National University, Canberra, Australia
FEBS J 274:4742-51. 2007..In this case, directed evolution has identified active site residues that destabilize the domain structure... - An unprecedented Fe(III)(mu-OH)Zn(II) complex that mimics the structural and functional properties of purple acid phosphatasesAdemir Neves
LABINC, , Universidade Federal de Santa Catarina, , SC, Brazil
J Am Chem Soc 129:7486-7. 2007 - Comparison between the geometric and electronic structures and reactivities of [FeNO]7 and [FeO2]8 complexes: a density functional theory studyGerhard Schenk
Department of Chemistry, Stanford University, Stanford, California 94305-5080, USA
J Am Chem Soc 126:505-15. 2004..Although NO is, in fact, harder to reduce, the resultant NO(-) species forms a more stable bond to Fe(III) relative to O(2)(-) due to the different bonding interactions... - Spectroscopic characterization of soybean lipoxygenase-1 mutants: the role of second coordination sphere residues in the regulation of enzyme activityGerhard Schenk
Department of Chemistry, Stanford University, California 94305-5080, USA
Biochemistry 42:7294-302. 2003..We propose that the H-bond between the weak Asn694 ligand and the Gln697 plays a key role in the modulation of the coordination flexibility of Asn694, and thus, is crucial for the regulation of enzyme reactivity...