original ) (raw )Fluorine-19 as a covalent active site-directed magnetic resonance probe in aspartate transaminase
Juan Slebe T.
Journal of Biological Chemistry, 1976
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Fluorinated amino acids and phosphopyridoxyl fluoroamino acids as reversible active site directed inhibitors of aspartate transaminase
M. Martinez-carrion , Juan Slebe T.
Biochemical and Biophysical Research Communications, 1975
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Carbamylation of aspartate transaminase and the pK value of the active site lysyl residue
M. Martinez-carrion
Journal of Biological Chemistry, 1976
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Specific labeling of the active site of cytosolic aspartate aminotransferase through the use of a cofactor analog N-(bromoacetyl)pyridoxamine
M. Martinez-carrion
Biochemistry, 1983
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Substrate Inhibition of d-Amino Acid Transaminase and Protection by Salts and by Reduced Nicotinamide Adenine Dinucleotide: Isolation and Initial Characterization of a Pyridoxo Intermediate Related to Inactivation
Dagmar Ringe
Biochemistry, 1998
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Properties of the active site lysyl residue of mitochondrial aspartate aminotransferase in solution
M. Martinez-carrion
The Journal of biological chemistry, 1983
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Effects of ligands and pH on the reactions of aspartate aminotransferase with aminooxyacetate and hydroxylamine
Raija Lindberg
Archives of Biochemistry and Biophysics, 1984
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Interaction of Pyridoxal 5‘-Phosphate with Tryptophan-139 at the Subunit Interface of Dimeric d -Amino Acid Transaminase †
Dagmar Ringe , Álvaro Martínez-del-Pozo , Gregory Petsko
Biochemistry, 1996
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Detection of Specific Solvent Rearrangement Regions of an Enzyme: NMR and ITC Studies with Aminoglycoside Phosphotransferase(3‘)-IIIa †
Engin Serpersu
Biochemistry, 2008
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Conformational changes of aspartate aminotransferases in the region of Cys-45 residue observed by means of spin label
Alexander Misharin
Biochimica et biophysica acta, 1973
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Location of exposed and buried cysteine residues in the polypeptide chain of aspartate aminotransferase
Sergey Deyev
FEBS Letters, 1973
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NMR Studies of Protonation and Hydrogen Bond States of Internal Aldimines of Pyridoxal 5′-Phosphate Acid–Base in Alanine Racemase, Aspartate Aminotransferase, and Poly-l-lysine
Hans-heinrich Limbach
Journal of the American Chemical Society, 2013
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1H NMR studies on the catalytic subunit of aspartate transcarbamoylase
H. Schachman
Proceedings of the National Academy of Sciences, 1992
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Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase
Álvaro Martínez-del-Pozo
Journal of Biological Chemistry
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13C NMR of enzymes
J. Malthouse
Progress in Nuclear Magnetic Resonance Spectroscopy, 1985
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Nuclear magnetic resonance studies of the active site of carboxypeptidase A
Gil Navon
Proceedings of the National Academy of Sciences, 1968
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Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine
Antoni Planas
1991
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Slowed Enzymatic Turnover Allows Characterization of Intermediates by Solid-State NMR †
Lynda McDowell
Biochemistry, 1997
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Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step
Mohammad Islam
Biochemistry, 2005
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Three-dimensional structure at 5 p resolution of cytosolic aspartate transaminase from chicken heart
Vsevolod Borisov
J Mol Biol, 1978
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Catalytic conformation of carboxypeptidase A
Devkumar Mustafi
Journal of Molecular Biology, 1983
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Characterization of the pH Titration Shifts of Ribonuclease A by One- and Two-Dimensional Nuclear Magnetic Resonance Spectroscopy
Agustin Kintanar
Archives of Biochemistry and Biophysics, 1996
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Nuclear magnetic resonance study of ligand binding to manganese-aspartate transcarbamylase
Sophie Chen
Biochemistry, 1975
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A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition
Kimberly Stieglitz
Journal of Molecular Biology, 2005
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The Isozymes of Glutamate-Aspartate Transaminase
M. Martinez-carrion
Journal of Biological Chemistry, 1970
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Use of 1 H− 15 N Heteronuclear Multiple-Quantum Coherence NMR Spectroscopy To Study the Active Site of Aspartate Aminotransferase †
Agustin Kintanar
Biochemistry, 1997
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Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction
wael rabeh
Archives of Biochemistry and Biophysics, 2008
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Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits
John Gerhart
Biochemistry, 1968
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NMR Studies of the Stability, Protonation States, and Tautomerism of 13C- and 15N-Labeled Aldimines of the Coenzyme Pyridoxal 5′-Phosphate in Water
Hans-heinrich Limbach
Biochemistry, 2010
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Crystal Structures and Solution Studies of Oxime Adducts of Mitochondrial Aspartate Aminotransferase
Alex Khomutov
European Journal of Biochemistry, 1996
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Effect of pH, ionic strength and univalent inorganic ions on the reconstitution of aspartate aminotransferase
Gennaro Marino
Biochemical Journal, 1974
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Active-site Arg → Lys Substitutions Alter Reaction and Substrate Specificity of Aspartate Aminotransferase
Sergio Giannattasio
Journal of Biological Chemistry, 1997
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Sensitive non-radioactive determination of aminotransferase stereospecificity for C-4′ hydrogen transfer on the coenzyme
JUNTRATIP JOMRIT
Biochemical and Biophysical Research Communications, 2011
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Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding
Gregory Petsko
Protein Science, 1995
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Crystal Structures of Aspartate Aminotransferase Reconstituted with 1-Deazapyridoxal 5′-Phosphate: Internal Aldimine and Stable l -Aspartate External Aldimine
Wait Griswold
Biochemistry, 2011
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