Primary Structure of Streptomyces griseus Metalloendopeptidase II

スポンサーリンク

概要

• 論文の詳細を見る

• Streptomyces griseus metalloendopeptidase II (SGMPII) is a unique protease, since it shows anomalous susceptibility to the proteinaceous"serine protease inhibitors"produced by Streptomyces, such as Streptomyces subtilisin inhibitor (SSI) and its homologous proteins. In this study, we analyzed the amino acid sequence of SGMPII by analyzing various peptide fragments produced enzymatically. The sequence of SGMPII, which is composed of 334 amino acids, showed no extensive similarity to SSI-insensitive metalloproteases produced by other species of Streptomyces, except for the amino acid residues essential for catalysis and zinc binding. However, SGMPII is 35-41% similar to thermolysin and its related metalloproteases, which are not inhibited by SSI, and the residues presumed to be critical for catalysis and zinc-binding are well conserved in SGMPII. Glu137 in a"His-Glu-Xaa-Xaa-His"motif of SGMPII was identified was the residue modified by ClCH_2 CO-DL-(N-OH) Leu-Ala-Gly-NH_2,an active-site-directed irreversible inhibitor of thermolysin-like metalloproteases. Based on the sequence comparison of SGMPII and other bacterial metalloproteases, we discuss the structural basis for the differences in substrate specificity and stability between SGMPII and other thermolysin-like proteases. A possible SSI-binding locus of SGMPII is also proposed.

• 社団法人日本農芸化学会の論文
• 1998-07-23

著者

• KOJIMA Shuichi

  Institute for Biomolecular Science, Gakushuin University

• MIURA Kin-ichiro

  Institute for Biomolecular Science, Gakushuin University

• Ishii Shinichi

  Faculty Of Pharmaceutical Sciences Hokkaido University

• KUMAZAKI Takashi

  Faculty of Pharmaceutical Sciences, Hokkaido University

• Kojima Shuichi

  Institute For Biomolecular Science Faculty Of Science Gakushuin University

• Kumazaki T

  Faculty Of Pharmaceutical Sciences Hokkaido University

• Miura Kin-ichiro

  Institute For Biomolecular Science Gakushuin Univ.:research Institute Chiba Institute Of Technology.

• Miura Kin-ichiro

  Institute For Biomolecular Science Faculty Of Science Gakushuin University

• Shuichi Kojima

  Institute for Biomolecular Science, Gakushuin University

関連論文

• High Performance in Refolding of Streptomyces griseus Trypsin by the Aid of a Mutant of Streptomyces Subtilisin Inhibitor Designed as Trypsin Inhibitor
• Cloning and Expression of the Catalase Gene from the Anaerobic Bacterium Desulfovibrio vulgaris (Miyazaki F)
• β-Glucosidase in the Indigo Plant : Intracellular Localization and Tissue Specific Expression in Leaves
• Purification and Characterization of a β-Glucosidase from Polygonum tinctorium, Which Catalyzes Preferentially the Hydrolysis of Indican
• Translational Regulation of the mRNA Encoding the Eukaryotic Translation Initiation Factor 4E in Xenopus
• Binding Analysis of Xenopus laevis Translation Initiation Factor 4E (eIF4E) in Initiation Complex Formation
• Cloning and Expression of the Gene Encoding Flavodoxin from Desulfovibrio vulgaris(Miyazaki F)^1
• Primary Structure of Streptomyces griseus Metalloendopeptidase II
• Structure-Activity Analysis of an Antimicrobial Peptide Derived from Bovine Apolipoprotein A-II
• Analysis of the Isoform of Xenopus Euakryotic Translation Initiation Factor 4E
• Polysomes of eukaryotic cells observed by electron microscopy
• Transmission electron and atomic force microscopic observation of polysomes on carbon-coated grids prepared by surface spreading
• The Effects of the Side Chains of Hydrophobic Aliphatic Amino Acid Residues in an Amphipathic Polypeptide on the Formation of α Helix and Its Association
• Quantitative in vitro Renaturation of Subtilisin BPN' without the Aid of Pro-sequence
• High Frequency of SSI-Like Protease Inhibitors among Streptomyces
• 1P193 Application of polarized IR-microscope spectroscopy and solid-state NMR to structural analysis of protein fibers(6. Macromolecular assembly,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
• Accelerated Refolding of Subtilisin BPN' by Tertiary-Structure-Forming Mutants of Its Propeptide^1
• Functional Tolerance of Streptomyces Subtilisin Inhibitor toward Conformational and Stability Changes Caused by Single-Point Mutations in the Hydrophobic Core
• 1P190 Toward creating metal binding helix fiber(6. Macromolecular assembly,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
• Codon and Base Biases after the Initiation Codon of the Open Reading Frames in the Escherichia coli Genome and Their Influence on the Translation Efficiency^1
• A Subtilisin Inhibitor Produced by Streptomyces bikiniensis Possesses a Glutamine Residue at Reactive Site P1
• An Endogenous Target Protease, SAM-P26, of Streptomyces Protease Inhibitor(SSI): Primary Structure, Enzymatic Characterizaion, and Its Interaction with SSI
• Fibril Formation by an Amphipathic α-Helix-Forming Polypeptide Produced by Gene Engineering
• The Effect of Hairpin DNA Fragments on Escherichia coli Poly(U)-Dependent Poly(Phe)Synthesis
• Inhibition of Translation and Progesterone-induced Maturation of Xenopus Oocytes by Expressing the Amino-terminal Portion of the Eukaryotic Translation Initiation Factor 4G(Biochemistry & Molecular Biology)
• Interference with Interaction between Eukaryotic Translation Initiation Factor 4G and Poly(A)-Binding Protein in Xenopus Oocytes Leads to Inhibition of Polyadenylated mRNA Translation and Oocyte Maturation
• Requirement of Ala Residues at g Position in Heptad Sequence of α-Helix-forming Peptide for Formation of Fibrous Structure
• Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II
• Introduction of Enzymatic Activity to .ALPHA.-Lactalbumin by Artificial Exon Shuffling.
• Binding Analysis of Xenopus laevis Translation Initiation Factor 4E (eIF4E) in Initiation Complex Formation.
• Functional Tolerance of Streptomyces Subtilisin Inhibitor toward Conformational and Stability Changes Caused by Single-Point Mutations in the Hydrophobic Core.
• Codon and Base Biases after the Initiation Codon of the Open Reading Frames in the Escherichia coli Genome and Their Influence on the Translation Efficiency.

もっと見る 閉じる

スポンサーリンク