Inactivation of Glutamate Racemase of Pediococcus pentosaceus with L-Serine O-Sulfate

スポンサーリンク

概要

• 論文の詳細を見る

• Glutamate racemase of Pediococcus pentosaceus catalyzes the α,β-elimination of L-serine O-sulfate to produce a pyruvate concomitantly with an irreversible inactivation of the enzyme. α,β-Elimination and inactivation reactions proceed through a common intermediate. L-Serine O-sulfate serves as a suicide substrate of the enzyme.

• 社団法人日本農芸化学会の論文
• 1993-11-23

著者

• Esaki N

  Institute For Chemical Research Kyoto University

• Esaki Nobuyoshi

  Kyoto Univ.

• Esaki Nobuyoshi

  Nstitute For Chemical Research Kyoto University

• Esaki Nobuyoshi

  Institute for Chemical Research, Kyoto University

• SODA Kenji

  Institute for Chemical Research, Kyoto University

• Yoshimura Tohru

  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya Uni

• Soda Kenji

  Department Of Biotechnology Kansai University

• Soda Kenji

  Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University

• Soda Kenji

  Institute For Chemical Resarch Kyoto University

• ASHIUCHI Makoto

  Institute for Chemical Research, Kyoto University

• Ashiuchi Makoto

  Department Of Bioresource Science Kochi University

• Ashiuchi Makoto

  Institute For Chemical Research Kyoto University

• Esaki Nobuyoshi

  Institute For Chemical Resarch Kyoto University

• Soda K

  Department Of Biotechnology Kansai University

• Ueno H

  Laboratory Of Biomacromolecular Chemistry Division Of Applied Life Sciences The Graduate School Of A

• Ueno Hiroshi

  Institute of Scientific and Industrial Research, Osaka University

• Yoshimura Tohru

  Department Of Applied Molecular Biosciences Graduate School Of Bioagricultural Sciences Nagoya Unive

関連論文

• Production of (S)-2-Chloropropionate by Asymmetric Reduction of 2-Chloroacrylate with 2-Haloacrylate Reductase Coupled with Glucose Dehydrogenase(BIOCHEMICAL ENGINEERING)
• Serine Racemase with Catalytically Active Lysinoalanyl Residue
• Amino Acid Racemases : Functions and Mechanisms
• Gene Cloning, Purification, and Characterization of 2, 3-Diaminopropionate Ammonia-lyase from Escherichia coli(Biochemistry & Molecular Biology)
• Stereospecificity for the Hydrogen Transfer of Pyridoxal Enzyme Reactions
• Gene Cloning, Purification, and Characterization of Two Cyanobacterial NifS Homologs Driving Iron-Sulfur Cluster Formation
• Stereochemistry of the Transamination Reaction Catalyzed by Aminodeoxychorismate Lyase from Escherichia coli: Close Relationship between Fold Type and Stereochemistry
• Three-Dimensional Structure of 4-Amino-4-Deoxychorismate Lyase from Escherichia coli
• Kinetic and Mutational Studies of Three NifS Homologs from Esherichia coli: Mechanistic Difference between L-Cysteine Desulfurase and L-Selenocysteine Lyase Reactions
• A Novel Zinc-containing α-Keto Ester Reductase from Actinomycete : An Approach Based on Protein Chemistry and Bioinformatics
• Mechanism of Inactivation of α-Amino-ε-caprolactam Racemase by α-Amino-δ -valerolactam
• Synthesis of Selenocystine and Selenohomocystine with O-Acetylhomoserine Sulfhydrylase
• Cloning and Expression of the Pseudomonas Gene for Utilization of D-Leucine in Escherichia coli
• Action of S-Carbamoyl and S-Thiocarbamoyl Derivatives of L-Cysteine on L-Amino Acid Oxidase
• Inactivation of Amino Acid Racemase by S-(N-Methylthiocarbamoyl)- D, L-cysteine
• Reactions of O-Substituted L-Homoserines Catalyzed by L-Methionine y-Lyase and Their Mechanism
• Purification and Properties of L-Methionine γ-Lyase from Aeromonas sp.
• Enzymatic Synthesis of S-Substituted L-Cysteines with Tryptophan Synthase of Escherichia coli
• Properties of α-Amino-ε-caprolactam Racemasefrom Achromobacter obae
• Catalysis-Linked Inactivation of Fluoroacetate Dehalogenase by Ammonia: A Novel Approach to Probe the Active-Site Environment
• X-Ray Structure of a Reaction Intermediate of L-2-Haloacid Dehalogenase with L-2-Chloropropionamid
• Primary Structure and Catalytic Properties of a Cold-active Esterase from a Psychrotroph, Acinetobacter sp. Strain No.6. Isolated from Siberian Soil(Biochemistry & Molecular Biology)
• Cold-Active Lipolytic Activity of Psychrotrophic Acinetobacter sp. Strain No.6
• Production of New Tricarboxylic Acid Anhydrides from Stearic Acid by Pseudomonas cepacia A-1419
• Biotransformation of Oleic Acid by Alcaligenes sp. 5-18,a Bacterium Tolerant to High Concentrations of Oleic Acid
• Biotransformation of Oleic Acid by Micrococcus luteus Cells
• Transformation of Oleic Acid and Its Esters by Sarcina lutea(Microbiology & Fermentation Industry)
• Identification of Proteins Interacting with Selenocysteine Lyase
• Thioredoxin Reductase 1 Is Important for Selenoprotein Biosynthesis in HeLa Cells
• Enzymatic Synthesis of L-Pipecolic Acid by Δ^1-Piperideine-2-carboxylate Reductase from Pseudomonas putida
• Selenoprotein Biosynthesis and Selenium-Specific Enzymes (特集1:若手が拓く微量元素研究の最前線)
• Protein Interaction between Selenophosphate Synthetase and IscS
• RNAi-mediated knock down of mammalian selenocysteine lyase
• A New Family of NAD(P)H-Dependent Oxidoreductases Distinct from Conventional Rossmann-Fold Proteins
• Network of Protein-Protein Interactions among Iron-Sulfur Cluster Assembly Proteins in Escherichia coli
• Structure of External Aldimine of Escherichia coli CsdB, an IscS/NifS Homolog: Implications for Its Specificity toward Selenocysteine
• Tyrosine 265 of Alanine Racemase Serves as a Base Abstracting α-Hydrogen from L-Alanine: The Counterpart Residue to Lysine 39 Specific to D-Alanine
• 2-Haloacrylate hydratase is a bifunctional enzyme with NADH-dependent FAD reductase activity
• Comprehensive Site-Directed Mutagenesis of L-2-Halo Acid Dehalogenase to Probe Catalytic Amino Acid Residues
• Two Kinds of 2-Halo Acid Dehalogenases from Pseudomonas sp. YL Induced by 2-Chloroacrylate and 2-Chloropropionate
• Role of Tyrosine 265 of Alanine Racemase from Bacillus stearothermophilus
• The Distribution of Phosphatidyl-D-serine in the Rat
• Primary Structure and Properties of Bacterial Formate Dehydrogenase From Moraxella sp C-1
• Thermostable Ornithine Aminotransferase from Bacillus sp. YM- 2: Purification and Characterization
• Structural Analysis of the L-Methionine γ-Lyase Gene from Pseudomonas putida^1
• Role of Leucine 201 of Thermostable D-Amino Acid Aminotransferase from a Thermophile, Bacillus sp. YM-1
• In Vivo Effect of GroESL on the Folding of Glutamate Racemase of Escherichia coli
• 364 Thermostable Formate Dehydrogenase from Mycobacterium vaccae N10; Structure and Function
• Large-Scale Production of Thermostable Alanine Dehydrogenase from Recombinant Cells
• Total Conversion of Racemic 2-Chloropropionic Acid into D-Lactate by Combination of Enzymatic and Chemical Dehalogenations
• 411 Enzymatic Dehalogenation of 2-Halo Acids in Nonaqueous Medium
• Characterization of Human Selenocysteine Synthase Involved in Selenoprotein Biosynthesis
• Functional Analysis of Two Homologous Mouse Selenophosphate Synthetases
• DnaK from Vibrio proteolyticus : Complementation of a dnaK-Null Mutant of Escherichia coli and the Role of Its ATPase Domain (Enzymology, Protein Engineering, and Enzyme Technology)
• Kinetics of Thermostable Alanine Racemase of Bacillus stearothermophilus
• Lysyl-tRNA Synthetase of Bacillus stearothermophilus Molecular Cloning and Expression of the Gene
• Crystal Structure of the Pyridoxal 5'-phosphate Dependent L-Methionine γ-Lyase from Pseudomonas putida
• Structure of the Antitumour Enzyme L-Methionine γ-Lyase from Pseudomonas putida at 1.8A Resolution
• Role of Tyrosine 114 of L-Methionine γ-lyase from Pseudomonas putida
• Transamination as a Side-Reaction catalyzed by Alanine Racemase of Bacillus stearothermophilus
• Construction and Properties of a Fragmentary D-Amino Acid Aminotransferase
• Stereospecific Labeling at α-Position of Phenylalanine and Phenylglycine with Amino Acid Racemase
• Compensation for D-Glutamate Auxotrophy of Escherichia coli WM335 by D-Amino Acid Aminotransferase Gene and Regulation of murI Expression
• Mutation of Arginine 98, Which Serves as a Substrate-Recognition Site of D-Amino Acid Aminotransferase, Can Be Partly Compensated for by Mutation of Tyrosine 88 to an Arginyl Residue
• Cloning and Expression of the Glutamate Racemase Gene of Bacillus pumilus^1
• Conversion of α-Keto Acids to D-Amino Acids by Coupling of Four Enzyme Reactions
• Glutamate Racemase of E. coli : Recharacterization of the Activation by UDP-N -Acetylmuramoyl-L-Alanine
• Reconstitution of Fragmentary Form of Thermostable Alanine Racemase
• A Novel NADH-Dependent Carbonyl Reductase from Kluyveromyces aestuarii and Comparison of NADH-Regeneration System for the Synthesis of Ethyl (S)-4-Chloro-3-hydroxybutanoate
• Catalytic Action of L-Methionine γ-Lyase on 4-Azaleucine(Biological Chemistry)
• Chemical Modification of Cysteine Residues of _L-Methionine γ-Lyase(Biological Chemistry)
• Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum
• Effects of Pyridoxal 5'-Phosphate on the Refolding of Aspartate Aminotransferase
• Limited Proteolysis of Thermostable Alanine Racemase of Bacillus stearothremophilus(Biological Chemistry)
• Stereospeciticity for the Hydrogen Transfer and Molecular Evolution of Pyridoxal Enzymes
• Inactivation of Glutamate Racemase of Pediococcus pentosaceus with L-Serine O-Sulfate
• Thermolabile Alanine Racemase from a Psychrotroph, Pseudomonas fluorescens : Purification and Properties
• Total Conversion of Racemic Pipecolic Acid into the L-Enantiomer by a Combination of Enantiospecific Oxidation with D-Amino Acid Oxidase and Reduction with Sodium Borohydride
• Synthesis of L-Proline form the Racemate by Coupling of Enzymatic Enantiospecific Oxidation and Chemical Non-Enantiospecific Reduction
• Decomposition of L-Selenodjenkolate Catalyzed by S-Alkylcysteine α,β-Lyase(Biological Chemistry)
• Continuous Conversion to Optically Pure L-Methionine from D-Enantiomer Contaminated Preparations by an Immobilized Enzyme Membrane Reactor
• Thermostable S-Alkylcysteine α,β-Lyase from a Thermophile : Purification and Properties(Biological Chemistry)
• Selenite Assimilation into Formate Dehydrogenase H Depends on Thioredoxin Reductase in Escherichia coli
• Gene Clonign, Purification, and Characterization of the Highly Thermostable Leucine Dehydrogenase of Bacillus sp.
• Gene Cloning, Purification and Characterization of Thermostable Alanine Dehydrogenase of Bacillus stearothermophilus
• Leucine Dehydrogenase of an Thermophilic Anaerobe, Clostridium thermoaceticum: Gene Cloning, Purification and Characterization(Microbiology & Fermentation Industry)
• The Role of Cysteine 116 in the Active Site of the Antitumor Enzyme L-Methionine γ-Lyase from Pseudomonas putida
• The Role of Cysteine 116 in the Active Site of the Antitumor Enzyme L-Methionine γ-Lyase from Pseudomonas putida
• The Distribution of Phosphatidyl-D-serine in the Rat
• Selenocysteine Is Selectively Taken Up by Red Blood Cells
• Identification of Proteins Interacting with Selenocysteine Lyase
• Expression analysis of mammalian selenocysteine lyase
• Determination by ^1H-NMR of the Stereospecificity of NAD-dependent Plant L-Histidinol Dehydrogenase for Nicotinamide C-4 Hydrogen Transfer
• Effects of Selenium Deficiency on the Expression of Selenoprotein mRNAs in Mouse Brain
• Specific transfer of selenium in selenoprotein biosynthesis
• Role of Cysteine Desulfurase in the Biosynthesis of Formate Dehydrogenase H Containing Mo, Molybdopterin, Selenocysteine, and Fe_4S_4 Cluster
• Protein Interaction between Selenocysteine Lyase and MUP-I
• The C_3-N Bond Cleavage of 2-Amino-3-(N-substituted-amino)-propionic Acids Catalyzed by L-Methionine γ-Lyase(Biological Chemistry)
• Mammalian Selenocysteine Lyase Is Involved in Selenoprotein Biosynthesis
• Selenite Reduction by the Thioredoxin System : Kinetics and Identification of Protein-Bound Selenide

もっと見る 閉じる

スポンサーリンク