Subsite Preferences of Pepstatin-Insensitive Carboxyl Proteinases from Bacteria.

スポンサーリンク

概要

• 論文の詳細を見る

• Pseudomonas sp. 101 carboxyl proteinase (PCP) and Xanthomonas sp. T-22 carboxyl proteinase (XCP), the first and second unique carboxyl proteinases from prokaryotes to be isolated and characterized, are not inhibited by the classical carboxyl proteinase inhibitor pepstatin. In this study, we elucidated their subsite preferences by using a series of synthetic chromogenic substrates, Lys-Pro-Ile(P3)-Glu(P2)-Phe*Nph-Arg(P2')-Leu(P3') (Nph is p-nitrophenylalanine, Phe*Nph is the cleavage site) with systematic substitutions at the P3, P2, P2', and P3' positions. Among 45 substrates tested, the best substrate for PCP had a Leu replacement at the P2 position (kcat=27.2 s-1, Km=4.22 μM, kcat/Km=6.43 μM-1•s-1), and that for XCP had an Ala replacement at the P3 position (kcat=79.4 s-1, Km=6.05 μM, kcat/Km=13.1 μM-1•s-1). PCP and XCP preferred such charged amino acid residues as Glu, Asp, Arg, or Lys at the P2' position. This suggested that the S2' subsites of PCP and XCP are occupied by hydrophilic residues, similar to that of pepstatin-insensitive carboxyl proteinase from Bacillus coagulans J-4 [Shibata et al. (1998) J. Biochem. 124, 642-647]. In contrast, the S2' subsite of pepstatin-sensitive carboxyl proteinases (aspartic proteinases) is hydrophobic in nature. Thus, the hydophilic nature of the S2' subsite appears to be a distinguishing feature of pepstatin-insensitive carboxyl proteinases.

• 社団法人 日本生化学会の論文

著者

• Oda Kohei

  Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture

• Dunn Ben

  Department Of Biochemistry And Molecular Biology University Of Florida

• Narutaki Shoji

  Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology

関連論文

• Cochinin B, a Novel Ribosome-Inactivating Protein from the Seeds of Momordica cochinchinensis(Biochemistry)
• High Molecular Weight Transglutaminase Inhibitor Produced by a Microorganism (Streptomyces lavendulae Y-200)
• Purification and Some Properties of an Inhibitor for a Yeast Pleiotropic Drug Resistant Pump from Kitasatospora sp. E-420(Biochemistry & Molecular Biology)
• A Novel Screening for Inhibitors of a Pleiotropic Drug Resistant Pump, Pdr5, in Saccharomyces cerevisiae(Biochemistry & Molecular Biology)
• Streptomyces Pepsin Inhibitor-insensitive Carboxyl Proteinase from Ganoderma lucidum
• Catalytic Residues and Substrate Specificity of Recombinant Human Tripeptidyl Peptidase I (CLN2)
• A CLN2-Related and Thermostable Serine-Carboxyl Proteinase, Kumamolysin: Cloning, Expression, and Identification of Catalytic Serine Residue
• Subsite Preferences of Pepstatin-Insensitive Carboxyl Proteinases from Prokaryotes: Kumamolysin, a Thermostable Pepstatin-Insensitive Carboxyl Proteinase^1
• A Simultaneous Assay Method for L-Glutamate and L-Pyroglutamate Contents in Soy Sauce Using a 5-Oxoprolinase (without ATP Hydrolyzing Activity)
• Isolation and Some Properties of a Novel Killer Toxin-like Protein Produced by Streptomyces sp. F-287
• Isolation and Some Properties of Sorbitol Oxidase from Streptomyces sp. H-7775
• Identification of Carboxyl Residues in Pepstatin-Insensitive Carboxyl Proteinase from Pseudomonas sp. 101 that Participate in Catalysis and Substrate Binding
• A Novel Metalloproteinase, Almelysin, from a Marine Bacterium, Alteromonas sp. No. 3696 : Purification and Characterization
• Substrate Specificity of a Novel Alcohol Resistant Metalloproteinase, Vimelysin, from Vibrio sp. T1800
• Cloining and Expression of an Isovaleryl Pepstatin-Insensitive Carboxyl Proteinase Gene from Xanthomonas sp. T-22
• A Novel Proteinaceous Kex 2 Proteinase Inhibitor, Kexstatin, from Streptomyces platensis Q268
• A Novel Alcohol Resistant Metalloproteinase, Vimelysin, from Vibrio sp. T1800: Purification and Characterization
• Isolation and Characterization of Chitinase from a Flake-chitin Degrading Marine Bacterium, Aeromonas hydrophila H-2330
• Molecular Cloning and Expression of a Gene Encoding a Novel Sorbitol Oxidase from Streptomyces sp.H-7775
• Additional Evidence for the Identity of Scytalidium lignicolum Acid Proteinases with the Carboxyl Proteinase Group : The Interaction between Angiotensin I and S-PI-Insensitive Acid Proteinases by Means of A Zinc(II)-Dye Complex as a Probe(Biological Chemi
• Characterization of the Complex between α_2-Macroglobulin and a Serine Proteinase from Bacillus natto(Biological Chemistry)
• Comparative Study on the Specificities of Several Fungal Aspartic and Acidic Proteinases towards the Tetradecapeptide of a Renin Substrate(Biological Chemistry)
• Carboxyl Proteinase Essential for Maturation of Basidiospores of Lentinus edodes (shiitake)
• Purification and Characterization of Glutamate Decarboxylase from Lactobacillus brevis IFO 12005
• Substrate Specificities of Pepstatin-Insensitive Carboxyl Proteinases from Gram-Negative Bacteria
• A Halophilic Serine Proteinase from Halobacillus sp. SR5-3 Isolated from Fish Sauce : Purification and Characterization
• Purification and Characterization of Serine Proteinase from a Halophilic Bacterium, Filobacillus sp. RF2-5
• Resynthesis of Reactive Site Peptide Bond and Temporary Inhibition of Streptomyces Metalloproteinase Inhibitor
• Identification of Reactive Site of a Proteinaceous Metalloproteinase Inhibitor from Streptomyces nigrescens TK-23
• Purification and Characterization of Cysteine Proteinase from a Baculovirus Gene
• Mutational Analysis of the Reactive Site Loop of Streptomyces Metalloproteinase Inhibitor, SMPI
• A Novel Thermostable, S-PI(Pepstatin Ac)-insensitive Acid Proteinase from Thermophilic Bacillus novosp. Strain MN-32(Biological Chemistry)
• The Primary Structure of Pepstatin-Insensitive Carboxyl Proteinase Produced by Pseudomonas sp. No. 101
• A Novel B-C-N Compound Derived from Melamine Diborate
• Subsite Prefernces of Pepstatin-Insensitive Carboxyl Proteinases from Bacteria
• Purification and Characterization of Alkaline Serine Proteinase from Photosynthetic Bacterium, Rubrivivax gelatinosus KDDS1
• An Alkaline Serine-Proteinase from a Bacterium Isolated from Bat Feces : Purification and Characterization
• Glutamate Decarboxylase from Lactobacillus brevis : Activation by Ammonium Sulfate
• Substrate Specificities and Kinetic Properties of Proteinase A from the Yeast Saccharomyces cerevisiae and the Development of a Novel Substrate
• Production of N-Acetyl-D-glucosamine from Chitin by Enzymatic Hydrolysis (特別企画 ミニレビュー特集)
• Structural Evidence That Scytalidolisin (Formerly Scytalidopepsin A) Is a Serine-Carboxyl Peptidase of the Sedolisin Family
• An Organic Solvent Resistant Tyrosinase from Streptomyces sp. REN-21 : Purification and Characterization
• High Temperature Corrosion of Refractories in Simulated Incinerator Ash under Hydrogen Chloride Gas
• Substrate Spercificity of Pepstatin-Insensitive Carboxyl Proteinase from Bacillus coagulans J-4
• Molecular Cloning of the Gene Encoding Vibrio Metalloproteinase Vimelysin and Isolation of a Mutant with High Stability in Organic Solvents
• High-Temperature Corrosion of Silicon Carbide in Simulated Waste Incinerator Ash
• Purification and Some Properties of Metal Proteinases from Lentinus edodes
• Kinetic Studies on S-PI(Pepstatin Ac)-insensitive Acid Proteinases of Scytalidium lignicolum ATCC 24568. Evidence Identifying Them with a Carboxyl Proteinase Group
• Purification and Some Properties of Carboxyl Proteinase in Extract from Lentinus edodes Fruit-bodies
• A CLN2-Related and Thermostable Serine-Carboxyl Proteinase, Kumamolysin: Cloning, Expression, and Identification of Catalytic Serine Residue.
• Subsite Preferences of Pepstatin-Insensitive Carboxyl Proteinases from Bacteria.
• Identification of Carboxyl Residues in Pepstatin-Insensitive Carboxyl Proteinase from Pseudomonas sp. 101 that Participate in Catalysis and Substrate Binding.

もっと見る 閉じる

スポンサーリンク