Mechanistic aspects of the transamination reactions catalyzed by D-amino acid transaminase from Haliscomenobacter hydrossis.

[1]  E. Y. Bezsudnova,et al.  The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme , 2021, Molecules.

[2]  Lijun Meng,et al.  Artificial Biocatalytic Cascade with Three Enzymes in One Pot for Asymmetric Synthesis of Chiral Unnatural Amino Acids , 2019, European Journal of Organic Chemistry.

[3]  F. Parmeggiani,et al.  One-Pot Biocatalytic Synthesis of Substituted d-Tryptophans from Indoles Enabled by an Engineered Aminotransferase , 2019, ACS Catalysis.

[4]  Uwe T. Bornscheuer,et al.  Biocatalytic Cascade Reaction for the Asymmetric Synthesis of L‐ and D‐Homoalanine , 2018, ChemCatChem.

[5]  F. Parmeggiani,et al.  Engineered Aminotransferase for the Production of d‐Phenylalanine Derivatives Using Biocatalytic Cascades , 2018 .

[6]  N. Ravin,et al.  Experimental and computational studies on the unusual substrate specificity of branched-chain amino acid aminotransferase from Thermoproteus uzoniensis. , 2016, Archives of biochemistry and biophysics.

[7]  L. Moe,et al.  Bacterial synthesis of d-amino acids , 2014, Applied Microbiology and Biotechnology.

[8]  H. Hayashi,et al.  Cloning and characterization of a novel fold-type I branched-chain amino acid aminotransferase from the hyperthermophilic archaeon Thermococcus sp. CKU-1 , 2014, Extremophiles.

[9]  J. Shin,et al.  Biocatalytic Asymmetric Synthesis of Unnatural Amino Acids through the Cascade Transfer of Amino Groups from Primary Amines onto Keto Acids , 2013 .

[10]  T. Ohshima,et al.  Characterization of d-amino acid aminotransferase from Lactobacillus salivarius , 2013 .

[11]  M. Toney.  Controlling reaction specificity in pyridoxal phosphate enzymes. , 2011, Biochimica et biophysica acta.

[12]  A. Paiardini,et al.  Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications. , 2007, The Biochemical journal.

[13]  M. M. Islam,et al.  Human Mitochondrial Branched Chain Aminotransferase Isozyme , 2006, Journal of Biological Chemistry.

[14]  M. Sung,et al.  Functional and Structural Characterization of Thermostable d-Amino Acid Aminotransferases from Geobacillus spp , 2006, Applied and Environmental Microbiology.

[15]  P. Cook,et al.  Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate. , 2005, Biochemistry.

[16]  Jack F Kirsch,et al.  Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. , 2003, Annual review of biochemistry.

[17]  H. Hayashi,et al.  Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme. , 2001, Biochemistry.

[18]  H. Hayashi,et al.  The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase. , 2000, Biochemistry.

[19]  Mizuguchi,et al.  The imine-pyridine torsion of the pyridoxal 5'-phosphate schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis , 1999, Biochemistry.

[20]  D. Ringe,et al.  Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. , 1998, Biochemistry.

[21]  G. Hammes.  A golden era for understanding enzyme mechanisms , 1998, Protein science : a publication of the Protein Society.

[22]  M. Toney,et al.  Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylase. , 1998, Biochemistry.

[23]  H Hayashi,et al.  Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism. , 1997, Journal of biochemistry.

[24]  H. Hayashi,et al.  Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase. , 1993, Biochemistry.

[25]  K. Soda,et al.  Characterization of the half and overall reactions catalyzed by L-lysine:2-oxoglutarate 6-aminotransferase. , 1991, Journal of biochemistry.

[26]  H. Hayashi,et al.  Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. , 1990, Biochemistry.

[27]  Shigehiro Asano,et al.  Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination. , 1989, The Journal of biological chemistry.

[28]  G. Eichele,et al.  Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. , 1984, Journal of molecular biology.

[29]  D. Metzler,et al.  Equilibriums and absorption spectra of Schiff bases , 1980 .

[30]  M. Cortijo,et al.  Studies on the pyridoxal phosphate site in glycogen phosphorylase b. , 1976, European journal of biochemistry.

[31]  K. Soda,et al.  D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties. , 1975, The Journal of biological chemistry.

[32]  A. Martell,et al.  Pyridoxine and Pyridoxal Analogs. VI. Electronic Absorption Spectra of Schiff Bases , 1963 .

[33]  S. Velick,et al.  A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism. , 1962, The Journal of biological chemistry.