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Structures and mechanisms of Nudix hydrolases.
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General theory of mortality and aging.
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Mechanisms of signaling and related enzymes
  • A. Mildvan
  • Biology, Chemistry
    Proteins
  • 1 December 1997
TLDR
From kinetic studies of mutant and metal ion substituted enzymes, the catalytic powers of cell signaling and related enzymes can be rationalized quantitatively by factors contributed by metal ion catalysis (≥105), general acid catalysis, general baseCatalysis, and transition‐state stabilization by cationic and hydrogen bond donating residues (≈103±1).
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Quantitative interpretations of double mutations of enzymes.
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15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
The solution secondary structure of 4-oxalocrotonate tautomerase (4-OT), a 41 kDa homohexamer with 62 residues per subunit, consists of an alpha-helix, two beta-strands, a beta-hairpin, two loops,…
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Inhibition of reverse transcription in vivo by elevated manganese ion concentration.
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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.
TLDR
The MgATP binding site of adenylate kinase, located by a combination of NMR and x-ray diffraction, is near three protein segments that are homologous in sequence to segments found in other nucleotide-binding phosphotransferases, suggesting equivalent mechanistic roles of these segments in all of these proteins.
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Probes of Structure and Function of Macromolecules and Membranes
TLDR
The probes of structure and function of macromolescules and membranes is one of the literary work in this world suitable to be reading material and will show the amazing benefits of reading a book.
Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action.
TLDR
On the basis of the structure of the quaternary complex, a mechanism of the MutT reaction is proposed which is qualitatively and quantitatively consistent with kinetic and mutagenesis studies and suggested that similar mechanisms may be operative for other enzymes that catalyze substitution at P(beta) of NTP substrates.
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Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates.
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