Nothing Special   »   [go: up one dir, main page]

Sakoh et al., 2005 - Google Patents

Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli

Sakoh et al., 2005

View HTML @Full View
Document ID
7926141100357004351
Author
Sakoh M
Ito K
Akiyama Y
Publication year
Publication venue
Journal of Biological Chemistry

External Links

Snippet

Escherichia coli HtpX is a putative membrane-bound zinc metalloprotease that has been suggested to participate in the proteolytic quality control of membrane proteins in conjunction with FtsH, a membrane-bound and ATP-dependent protease. Here, we …
Continue reading at www.jbc.org (HTML) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/113—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing
    • C12N15/1137—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing against enzymes
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing

Similar Documents

Publication Publication Date Title
Sakoh et al. Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli
Berkmen et al. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
Choi-Rhee et al. The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase
Roche et al. Identification of endogenous SsrA-tagged proteins reveals tagging at positions corresponding to stop codons
Yokota et al. Characterization of the LolA-LolB system as the general lipoprotein localization mechanism of Escherichia coli
Akiyama et al. RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
Kimura et al. N α-acetylation and proteolytic activity of the yeast 20 S proteasome
Bessette et al. In Vivo and in Vitro Function of theEscherichia coli Periplasmic Cysteine Oxidoreductase DsbG
Matsushita et al. A Study of the Collagen-binding Domain of a 116-kDaClostridium histolyticum Collagenase
Jiang et al. Chloroplast YidC homolog Albino3 can functionally complement the bacterial YidC depletion strain and promote membrane insertion of both bacterial and chloroplast thylakoid proteins
Richter et al. A chloroplast processing enzyme functions as the general stromal processing peptidase
Schliebs et al. Recombinant human peroxisomal targeting signal receptor PEX5: structural basis for interaction of PEX5 with PEX14
Hanawa-Suetsugu et al. SmpB functions in various steps of trans-translation
Tanaka et al. RtcB is the RNA ligase component of an Escherichia coli RNA repair operon
Chon et al. Contributions of the two accessory subunits, RNASEH2B and RNASEH2C, to the activity and properties of the human RNase H2 complex
Winter et al. Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
Bernard et al. BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance
Barnett et al. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
White et al. A Novel Activity of OmpT.: PROTEOLYSIS UNDER EXTREME DENATURING CONDITIONS∗
Hanai et al. Molecular dissection of a protein SopB essential for Escherichia coli F plasmid partition
Huang et al. The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli
Kanemori et al. Marked Instability of the ς32 Heat Shock Transcription Factor at High Temperature: IMPLICATIONS FOR HEAT SHOCK REGULATION
Terziyska et al. Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria
Schmidt et al. Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
Li et al. Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter