JP2005505250A - 核酸およびチオレドキシンレダクターゼ活性を有するタンパク質 - Google Patents

核酸およびチオレドキシンレダクターゼ活性を有するタンパク質 Download PDF

Info

Publication number
JP2005505250A
JP2005505250A JP2002587384A JP2002587384A JP2005505250A JP 2005505250 A JP2005505250 A JP 2005505250A JP 2002587384 A JP2002587384 A JP 2002587384A JP 2002587384 A JP2002587384 A JP 2002587384A JP 2005505250 A JP2005505250 A JP 2005505250A
Authority
JP
Japan
Prior art keywords
protein
seq
polypeptide
mutant
amino acid
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
JP2002587384A
Other languages
English (en)
Japanese (ja)
Other versions
JP2005505250A5 (enExample
Inventor
スティーブン・ピー・ブリッグズ
ビピン・ケイ・ダルミア
グレゴリー・デル・バル
ジョン・アール・デスジャーレイス
ピーター・ハイフェッツ
ピーター・ルジンブール
ウメシュ・マッチハル
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Syngenta Participations AG
Xencor Inc
Original Assignee
Syngenta Participations AG
Xencor Inc
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Syngenta Participations AG, Xencor Inc filed Critical Syngenta Participations AG
Publication of JP2005505250A publication Critical patent/JP2005505250A/ja
Publication of JP2005505250A5 publication Critical patent/JP2005505250A5/ja
Pending legal-status Critical Current

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
    • C12N9/0036—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on NADH or NADPH (1.6)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; 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
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; 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
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
    • C12N15/8257—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y108/00—Oxidoreductases acting on sulfur groups as donors (1.8)
    • C12Y108/01—Oxidoreductases acting on sulfur groups as donors (1.8) with NAD+ or NADP+ as acceptor (1.8.1)
    • C12Y108/01009—Thioredoxin-disulfide reductase (1.8.1.9), i.e. thioredoxin-reductase
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A90/00—Technologies having an indirect contribution to adaptation to climate change
    • Y02A90/10—Information and communication technologies [ICT] supporting adaptation to climate change, e.g. for weather forecasting or climate simulation

Landscapes

  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Molecular Biology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Microbiology (AREA)
  • Cell Biology (AREA)
  • Plant Pathology (AREA)
  • Biophysics (AREA)
  • Physics & Mathematics (AREA)
  • Medicinal Chemistry (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Peptides Or Proteins (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Information Retrieval, Db Structures And Fs Structures Therefor (AREA)
  • Fodder In General (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
JP2002587384A 2001-05-04 2002-05-06 核酸およびチオレドキシンレダクターゼ活性を有するタンパク質 Pending JP2005505250A (ja)

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
US28902901P 2001-05-04 2001-05-04
US37060902P 2002-04-05 2002-04-05
US37668202P 2002-04-29 2002-04-29
PCT/US2002/014358 WO2002090300A2 (en) 2001-05-04 2002-05-06 Nucleic acids and proteins with thioredoxin reductase activity

Publications (2)

Publication Number Publication Date
JP2005505250A true JP2005505250A (ja) 2005-02-24
JP2005505250A5 JP2005505250A5 (enExample) 2005-09-15

Family

ID=30119062

Family Applications (1)

Application Number Title Priority Date Filing Date
JP2002587384A Pending JP2005505250A (ja) 2001-05-04 2002-05-06 核酸およびチオレドキシンレダクターゼ活性を有するタンパク質

Country Status (5)

Country Link
US (2) US7071307B2 (enExample)
EP (1) EP1507852A4 (enExample)
JP (1) JP2005505250A (enExample)
CA (1) CA2447407A1 (enExample)
WO (1) WO2002090300A2 (enExample)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8460925B2 (en) 2004-10-15 2013-06-11 Monell Chemical Senses Center Methods for culturing mammalian taste cells
WO2022270588A1 (ja) * 2021-06-23 2022-12-29 パナソニックＩｐマネジメント株式会社 融合タンパク質、融合タンパク質の製造方法、電極、酸化還元装置、酸化還元方法、ジスルフィド結合の切断方法、及び、アレルゲンの不活化方法

Families Citing this family (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20030211511A1 (en) * 2001-05-04 2003-11-13 Briggs Steven P. Nucleic acids and proteins with thioredoxin reductase activity
EP1507852A4 (en) * 2001-05-04 2005-12-28 Xencor Inc NUCLEIC ACIDS AND PROTEINS WITH THIORODOXIN REDUCED EFFECT
WO2004024868A2 (en) * 2002-09-10 2004-03-25 National Jewish Medical And Research Center Product and process for liquefaction of mucus or sputum
EP1633865B1 (en) 2003-06-18 2011-09-28 Bayer Pharma Aktiengesellschaft New biological entities and the use thereof
EP1829968A4 (en) * 2004-12-20 2008-09-10 Ajinomoto Kk PROTEIN MUTANT WITH PEPTIDE PRODUCTION ACTIVITY
WO2012075911A1 (zh) * 2010-12-06 2012-06-14 Li Jianyuan 重组人prx-6蛋白在治疗烧烫伤和/或角膜损伤中的用途
AU2014232520B2 (en) * 2013-03-15 2019-04-04 Orpro Therapeutics, Inc. Product and process for mucus viscosity normalization
CN105671012A (zh) * 2016-04-13 2016-06-15 深圳大学 一种雨生红球藻硒蛋白及其编码基因与应用
CN115778837B (zh) * 2022-11-21 2024-04-02 安徽品赫生物科技有限公司 一种协同增效的亮肤修护冻干粉及其制备方法和应用

Family Cites Families (33)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5646016A (en) * 1991-02-06 1997-07-08 Genetics Institute, Inc. Peptide and protein fusions to thioredoxin, thioredoxin-like molecules, and modified thioredoxin-like molecules
DE4133644A1 (de) * 1991-10-11 1993-04-15 Nukem Gmbh Halbleiterbauelement, verfahren zu dessen herstellung sowie hierzu benutzte anordnung
US5952034A (en) 1991-10-12 1999-09-14 The Regents Of The University Of California Increasing the digestibility of food proteins by thioredoxin reduction
CA2121137A1 (en) * 1991-10-12 1993-04-29 Bob B. Buchanan Use of thiol redox proteins for reducing disulfide bonds
EP1255209A3 (en) 1997-04-11 2009-02-11 California Institute Of Technology Apparatus and method for automated protein design
JP2002510966A (ja) 1997-04-11 2002-04-09 カリフォルニア・インスティテュート・オブ・テクノロジー 自動蛋白質デザインのための装置および方法
US7585645B2 (en) 1997-05-27 2009-09-08 Sembiosys Genetics Inc. Thioredoxin and thioredoxin reductase containing oil body based products
US20020048772A1 (en) 2000-02-10 2002-04-25 Dahiyat Bassil I. Protein design automation for protein libraries
AU774334B2 (en) 1998-10-16 2004-06-24 Xencor Protein design automation for protein libraries
US7315786B2 (en) 1998-10-16 2008-01-01 Xencor Protein design automation for protein libraries
US6403312B1 (en) 1998-10-16 2002-06-11 Xencor Protein design automatic for protein libraries
US20030049654A1 (en) 1998-10-16 2003-03-13 Xencor Protein design automation for protein libraries
EP1033405A3 (en) * 1999-02-25 2001-08-01 Ceres Incorporated Sequence-determined DNA fragments and corresponding polypeptides encoded thereby
AU770629B2 (en) * 1999-03-31 2004-02-26 Regents Of The University Of California, The Barley gene for thioredoxin and NADP-thioredoxin reductase
DK1255826T3 (da) 2000-02-10 2006-01-30 Xencor Inc Automatisering af proteindesign for proteinbiblioteker
US6423518B1 (en) 2000-09-11 2002-07-23 Rutgers, The State University Design and production of mutant 2,5-diketo-D-gluconic acid reductase enzymes with altered cofactor dependency
US6576452B1 (en) 2000-10-04 2003-06-10 Genencor International, Inc. 2,5-diketo-L-gluconic acid reductases and methods of use
US20090197337A1 (en) * 2000-12-19 2009-08-06 Van Rooijen Gijs Methods for the production of multimeric proteins and related compositions
US20030211511A1 (en) 2001-05-04 2003-11-13 Briggs Steven P. Nucleic acids and proteins with thioredoxin reductase activity
EP1507852A4 (en) * 2001-05-04 2005-12-28 Xencor Inc NUCLEIC ACIDS AND PROTEINS WITH THIORODOXIN REDUCED EFFECT
US20030130827A1 (en) 2001-08-10 2003-07-10 Joerg Bentzien Protein design automation for protein libraries
AU2003226032A1 (en) * 2002-04-11 2003-10-27 The Regents Of The University Of California Low allergen plant and animal genotypes
US8014867B2 (en) * 2004-12-17 2011-09-06 Cardiac Pacemakers, Inc. MRI operation modes for implantable medical devices
US7917213B2 (en) * 2005-11-04 2011-03-29 Kenergy, Inc. MRI compatible implanted electronic medical lead
US7729770B2 (en) * 2006-04-26 2010-06-01 Medtronic, Inc. Isolation circuitry and method for gradient field safety in an implantable medical device
US7610101B2 (en) * 2006-11-30 2009-10-27 Cardiac Pacemakers, Inc. RF rejecting lead
US9345888B2 (en) * 2007-03-09 2016-05-24 Cardiac Pacemakers, Inc. MRI compatible implantable medical devices and methods
US8086321B2 (en) * 2007-12-06 2011-12-27 Cardiac Pacemakers, Inc. Selectively connecting the tip electrode during therapy for MRI shielding
US8032228B2 (en) * 2007-12-06 2011-10-04 Cardiac Pacemakers, Inc. Method and apparatus for disconnecting the tip electrode during MRI
US8311637B2 (en) * 2008-02-11 2012-11-13 Cardiac Pacemakers, Inc. Magnetic core flux canceling of ferrites in MRI
US8160717B2 (en) * 2008-02-19 2012-04-17 Cardiac Pacemakers, Inc. Model reference identification and cancellation of magnetically-induced voltages in a gradient magnetic field
US8571661B2 (en) * 2008-10-02 2013-10-29 Cardiac Pacemakers, Inc. Implantable medical device responsive to MRI induced capture threshold changes
EP2398553B1 (en) * 2009-02-19 2015-07-22 Cardiac Pacemakers, Inc. Systems for providing arrhythmia therapy in mri environments

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8460925B2 (en) 2004-10-15 2013-06-11 Monell Chemical Senses Center Methods for culturing mammalian taste cells
WO2022270588A1 (ja) * 2021-06-23 2022-12-29 パナソニックＩｐマネジメント株式会社 融合タンパク質、融合タンパク質の製造方法、電極、酸化還元装置、酸化還元方法、ジスルフィド結合の切断方法、及び、アレルゲンの不活化方法

Also Published As

Publication number Publication date
EP1507852A4 (en) 2005-12-28
CA2447407A1 (en) 2002-11-14
EP1507852A2 (en) 2005-02-23
US20060149482A1 (en) 2006-07-06
WO2002090300A8 (en) 2004-04-22
US20030100743A1 (en) 2003-05-29
WO2002090300A2 (en) 2002-11-14
US7071307B2 (en) 2006-07-04
WO2002090300A3 (en) 2004-12-09

Similar Documents

Publication Publication Date Title
Liu et al. Functional divergence of the glutathione S-transferase supergene family in Physcomitrella patens reveals complex patterns of large gene family evolution in land plants
Robinson et al. Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases
Williams et al. P1B-ATPases–an ancient family of transition metal pumps with diverse functions in plants
Read et al. High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial RubiSCO containing" algal" residue modifications
Fomenko et al. Identity and functions of CxxC-derived motifs
Buchanan et al. Redox regulation: a broadening horizon
EP2904101B1 (en) Intein-modified proteases, their production and industrial applications
Acharya et al. Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase
Esser et al. Plant and animal glycolate oxidases have a common eukaryotic ancestor and convergently duplicated to evolve long-chain 2-hydroxy acid oxidases
Mestres-Ortega et al. The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin
US7071307B2 (en) Nucleic acids and proteins with thioredoxin reductase activity
CN101553499A (zh) 蛋白产生方法及其用途
Rho et al. Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis
Gollan et al. Genome-wide analysis of genes encoding FK506-binding proteins in rice
Selles et al. Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
Verma et al. OsAlba1, a dehydration-responsive nuclear protein of rice (Oryza sativa L. ssp. indica), participates in stress adaptation
Kolahi et al. In silico prediction, phylogenetic and bioinformatic analysis of SoPCS gene, survey of its protein characterization and gene expression in response to cadmium in Saccharum officinarum
Carrillo et al. Assembly of plant ferredoxin-NADP+ oxidoreductase in Escherichia coli requires GroE molecular chaperones.
WO2013138351A1 (en) Separatome-based protein expression and purification platform
US20030211511A1 (en) Nucleic acids and proteins with thioredoxin reductase activity
Saha et al. Characterization of the evolutionarily conserved iron–sulfur cluster of sirohydrochlorin ferrochelatase from Arabidopsis thaliana
Okumura et al. A novel protein in Photosystem II of a diatom Chaetoceros gracilis is one of the extrinsic proteins located on lumenal side and directly associates with PSII core components
Purty et al. Structural and expression analysis of salinity stress responsive phosphoserine phosphatase from Brassica juncea L
Farmani et al. Conjugated linoleic acid‐producing enzymes: A bioinformatics study
Nelapati et al. Computational analysis of therapeutic enzyme uricase from different source organisms

Legal Events

Date Code Title Description
A131 Notification of reasons for refusal

Free format text: JAPANESE INTERMEDIATE CODE: A131

Effective date: 20060131

A02 Decision of refusal

Free format text: JAPANESE INTERMEDIATE CODE: A02

Effective date: 20060815