Search Results - "MILDVAN, A. S"

Structures and mechanisms of Nudix hydrolases by Mildvan, A.S., Xia, Z., Azurmendi, H.F., Saraswat, V., Legler, P.M., Massiah, M.A., Gabelli, S.B., Bianchet, M.A., Kang, L.-W., Amzel, L.M.

“…Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates linked to other moieties, X , and contain the sequence motif or Nudix box, GX 5EX…”
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ATP-Binding Site of Adenylate Kinase: Mechanistic Implications of Its Homology with ras-Encoded p21, F1-ATPase, and Other Nucleotide-Binding Proteins by Fry, David C., Kuby, Stephen A., Mildvan, Albert S.

“…The MgATP binding site of adenylate kinase, located by a combination of NMR and x-ray diffraction, is near three protein segments, five to seven amino acids in…”
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NMR Evidence for a Short, Strong Hydrogen Bond at the Active Site of a Cholinesterase by Viragh, Carol, Harris, Thomas K, Reddy, Putta Mallikarjuna, Massiah, Michael A, Mildvan, Albert S, Kovach, Ildiko M

“…Cholinesterases (ChE), use a Glu−His−Ser catalytic triad to enhance the nucleophilicity of the catalytic serine. It has been shown that serine proteases, which…”
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Mechanistic Implications of Methylglyoxal Synthase Complexed with Phosphoglycolohydroxamic Acid As Observed by X-ray Crystallography and NMR Spectroscopy by Marks, Gregory T, Harris, Thomas K, Massiah, Michael A, Mildvan, Albert S, Harrison, David H. T

“…Methylglyoxal synthase (MGS) and triosephosphate isomerase (TIM) share neither sequence nor structural similarities, yet the reactions catalyzed by both…”
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Mechanisms of signaling and related enzymes by Mildvan, Albert S.

“…Most enzymes involved in cell signaling, such as protein kinases, protein phosphatases, GTPases, and nucleotide cyclases catalyze nucleophilic substitutions at…”
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Vaccinia DNA topoisomerase I: Single-turnover and steady-state kinetic analysis of the DNA strand cleavage and ligation reactions by Stivers, James T, Shuman, Stewart, Mildvan, Albert S

“…Vaccinia DNA topoisomerase I catalyzes a reversible, site-specific strand cleavage and resealing reaction with duplex DNA involving a transient…”
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Dual divalent cation requirement of the MutT dGTPase. Kinetic and magnetic resonance studies of the metal and substrate complexes by FRICK, D. N, WEBER, D. J, GILLESPIE, J. R, BESSMAN, M. J, MILDVAN, A. S

“…Kinetic analyses of both the Mn(2+)- and Mg(2+)-activated hydrolysis of dGTP by MutT show the requirement for two divalent cations. Whereas Mn2+ supports a…”
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Substrate and DNA binding to a 50-residue peptide fragment of DNA polymerase I. Comparison with the enzyme by MULLEN, G. P, SHENBAGAMURTHI, P, MILDVAN, A. S

“…The fluorescent nucleotide 2',3'-trinitrophenyl-ATP (TNP-ATP) binds at the triphosphate substrate binding site of the large (Klenow) fragment of DNA polymerase…”
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The Structural Basis for the Perturbed pKa of the Catalytic Base in 4-Oxalocrotonate Tautomerase:  Kinetic and Structural Effects of Mutations of Phe-50 by CZERWINSKI, Robert M., HARRIS, Thomas K., MASSIAH, Michael A., MILDVAN, Albert S., WHITMAN, Christian P.

“…The amino-terminal proline of 4-oxalocrotonate tautomerase (4-OT) functions as the general base catalyst in the enzyme-catalyzed isomerization of…”
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High-Precision Measurement of Hydrogen Bond Lengths in Proteins by Nuclear Magnetic Resonance Methods by Harris, Thomas K., Mildvan, Albert S.

“…We have compared hydrogen bond lengths on enzymes derived with high precision (≤ ±0.05 Å) from both the proton chemical shifts (δ) and the fractionation…”
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Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis by Serpersu, Engin H, Shortle, David, Mildvan, Albert S

“…To determine the origin of the overall approximately 10(16)-fold rate enhancement of DNA hydrolysis catalyzed by staphylococcal nuclease, the effects of single…”
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Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants by Serpersu, E. H, McCracken, J, Peisach, J, Mildvan, A. S

“…Electron spin echo envelope modulation (ESEEM) spectroscopy has been applied to the determination of the number of water molecules coordinated to the metal in…”
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NMR docking of a substrate into the X-ray structure of staphylococcal nuclease by Weber, D J, Gittis, A G, Mullen, G P, Abeygunawardana, C, Lattman, E E, Mildvan, A S

“…The conformation of the staphylococcal nuclease-bound metal-dTdA complex, previously determined by NMR methods [Weber, D.J., Mullen, G.P., Mildvan, A.S. (1991)…”
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NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme by FRY, D. C, KUBY, S. A, MILDVAN, A. S

“…Proton NMR was used to study the interaction of beta,gamma-bidentate Cr3+ATP and MgATP with rabbit muscle adenylate kinase, which has 194 amino acids, and with…”
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Interactions of the acid and base catalysts on staphylococcal nuclease as studied in a double mutant by Weber, David J, Meeker, Alan K, Mildvan, Albert S

“…The mechanism of the phosphodiesterase reaction catalyzed by staphylococcal nuclease is believed to involve concerted general acid-base catalysis by Arg-87 and…”
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4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy by Stivers, James T., Abeygunawardana, Chitrananda, Whitman, Christian P., Mildvan, Albert S.

“…4‐Oxalocrotonate tautomerase (4‐OT), a homohexamer consisting of 62 residues per subunit, catalyzes the isomerization of unsaturated α‐keto acids using Pro‐1…”
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Metal binding to DNA polymerase I, its large fragment, and two 3',5'-exonuclease mutants of the large fragment by MULLEN, G. P, SERPERSU, E. H, FERRIN, L. J, LOEB, L. A, MILDVAN, A. S

“…DNA polymerase I (Pol I) is an enzyme of DNA replication and repair containing three active sites, each requiring divalent metal ions such as Mg2+ or Mn2+ for…”
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NMR studies of the interactions of substrates with enzymes and their peptide fragments by Mildvan, A S

“…Metal-nucleus distances measured by paramagnetic effects on T1 and interproton distances measured by the nuclear Overhauser effect have been used to determine…”
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Solution structure and mechanism of the MutT pyrophosphohydrolase by Mildvan, A S, Weber, D J, Abeygunawardana, C

“…The MutT enzyme prevents errors in DNA replication by hydrolyzing mutagenic nucleotide substrates such as 8-oxo-dGTP. It does so by catalyzing nucleophilic…”
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Secondary structure of the MutT enzyme as determined by NMR by Weber, David J., Abeygunawardana, Chitrananda, Bessman, Maurice J., Mildvan, Albert S.

“…The MutT enzyme (129 amino acids) catalyzes the hydrolysis of nucleoside triphosphates (NTP) to nucleotides (NMP) and pyrophosphate by nucleophilic…”
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