CA3042231A1 - Compositions and methods for the production of compounds - Google Patents
Compositions and methods for the production of compounds Download PDFInfo
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- CA3042231A1 CA3042231A1 CA3042231A CA3042231A CA3042231A1 CA 3042231 A1 CA3042231 A1 CA 3042231A1 CA 3042231 A CA3042231 A CA 3042231A CA 3042231 A CA3042231 A CA 3042231A CA 3042231 A1 CA3042231 A1 CA 3042231A1
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- polyketide synthase
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Classifications
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/44—Preparation of O-glycosides, e.g. glucosides
- C12P19/60—Preparation of O-glycosides, e.g. glucosides having an oxygen of the saccharide radical directly bound to a non-saccharide heterocyclic ring or a condensed ring system containing a non-saccharide heterocyclic ring, e.g. coumermycin, novobiocin
- C12P19/62—Preparation of O-glycosides, e.g. glucosides having an oxygen of the saccharide radical directly bound to a non-saccharide heterocyclic ring or a condensed ring system containing a non-saccharide heterocyclic ring, e.g. coumermycin, novobiocin the hetero ring having eight or more ring members and only oxygen as ring hetero atoms, e.g. erythromycin, spiramycin, nystatin
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- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
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- 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
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
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- 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
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/1029—Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P17/00—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms
- C12P17/18—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms containing at least two hetero rings condensed among themselves or condensed with a common carbocyclic ring system, e.g. rifamycin
- C12P17/188—Heterocyclic compound containing in the condensed system at least one hetero ring having nitrogen atoms and oxygen atoms as the only ring heteroatoms
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- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Enzymes And Modification Thereof (AREA)
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| US201662414435P | 2016-10-28 | 2016-10-28 | |
| US62/414,435 | 2016-10-28 | ||
| PCT/US2017/058805 WO2018081592A2 (en) | 2016-10-28 | 2017-10-27 | Compositions and methods for the production of compounds |
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| EP4085933A3 (en) | 2016-04-12 | 2023-01-11 | Ginkgo Bioworks, Inc. | Compositions and methods for the production of compounds |
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| AU2020379731A1 (en) | 2019-11-04 | 2022-05-05 | Revolution Medicines, Inc. | Ras inhibitors |
| WO2021091956A1 (en) | 2019-11-04 | 2021-05-14 | Revolution Medicines, Inc. | Ras inhibitors |
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| US10947552B1 (en) | 2020-09-30 | 2021-03-16 | Alpine Roads, Inc. | Recombinant fusion proteins for producing milk proteins in plants |
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| ES2089723T3 (es) | 1992-03-27 | 1996-10-01 | American Home Prod | 29-demetoxirapamicina para inducir la inmunodepresion. |
| DK0725778T3 (da) | 1993-09-20 | 2001-12-17 | Univ Leland Stanford Junior | Rekombinant produktion af hidtil ukendte polyketider |
| IL112873A (en) | 1994-03-08 | 2005-03-20 | Wyeth Corp | Rapamycin-fkbp12 binding proteins, their isolation and their use |
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| ATE473759T1 (de) | 1998-05-22 | 2010-07-15 | Univ Leland Stanford Junior | Bifunktionelle moleküle sowie darauf basierende therapien. |
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| US6686454B1 (en) | 1998-10-09 | 2004-02-03 | Isotechnika, Inc. | Antibodies to specific regions of cyclosporine related compounds |
| CA2359801A1 (en) | 1999-02-09 | 2000-08-17 | Rajesh S. Gokhale | Methods to mediate polyketide synthase module effectiveness |
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| US7220552B1 (en) | 1999-11-19 | 2007-05-22 | The Board Of Trustees Of The Leland Stanford Junior University | Bifunctional molecules and their use in the disruption of protein-protein interactions |
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| MXPA02000823A (es) | 2000-05-23 | 2002-07-30 | Vertex Pharma | Inhibidores de caspasa y uso de los mismos. |
| US7198924B2 (en) * | 2000-12-11 | 2007-04-03 | Invitrogen Corporation | Methods and compositions for synthesis of nucleic acid molecules using multiple recognition sites |
| US20030153053A1 (en) * | 2001-08-06 | 2003-08-14 | Ralph Reid | Methods for altering polyketide synthase genes |
| US6809077B2 (en) | 2001-10-12 | 2004-10-26 | Enanta Pharmaceuticals, Inc. | Cyclosporin analogs for the treatment of autoimmune diseases |
| US6987090B2 (en) | 2002-05-09 | 2006-01-17 | Lg Household & Health Care Ltd. | Use of 3-position cyclosporin derivatives for hair growth |
| EP1477563A3 (en) * | 2003-05-16 | 2004-11-24 | Wyeth | Cloning genes from streptomyces cyaneogriseus subsp.noncyanogenus for biosynthesis of antibiotics and methods of use |
| JP2009528292A (ja) | 2006-02-27 | 2009-08-06 | ザ ボード オブ トラスティーズ オブ レランド スタンフォード ジュニア ユニバーシティ | 生物学的障壁を越える増強された放出特性を有する分子の輸送のための組成物および方法 |
| US20070203168A1 (en) | 2006-02-28 | 2007-08-30 | Zhao Jonathon Z | Isomers of rapamycin and 42-Epi-rapamycin, methods of making and using the same |
| KR100945483B1 (ko) | 2007-10-25 | 2010-03-05 | 이화여자대학교 산학협력단 | ｐｉｋＤ 조절유전자의 발현벡터를 이용한 스트렙토미세스베네주엘라에（Ｓｔｒｅｐｔｏｍｙｃｅｓｖｅｎｅｚｕｅｌａｅ）에서폴리케타이드（ｐｏｌｙｋｅｔｉｄｅ）의 생산성 증가방법 |
| GB0805363D0 (en) * | 2008-03-20 | 2008-04-30 | Sinvent As | Novel NRPS-PKS gene cluster and its manipulation and utility |
| WO2010031185A1 (en) | 2008-09-19 | 2010-03-25 | Protox Therapeutics Inc. | Treating cancer stem cells using targeted cargo proteins |
| US8962329B2 (en) | 2008-09-24 | 2015-02-24 | Shanghai Institute Of Organic Chemistry, Chinese Academy Of Sciences | Gene cluster |
| WO2010088573A1 (en) | 2009-01-30 | 2010-08-05 | Enanta Pharmaceuticals, Inc. | Cyclosporin analogues for preventing or treating hepatitis c infection |
| WO2011008260A2 (en) | 2009-07-13 | 2011-01-20 | President And Fellows Of Harvard College | Bifunctional stapled polypeptides and uses thereof |
| WO2011009938A2 (en) | 2009-07-24 | 2011-01-27 | Universite Henri Poincare Nancy 1 | Stambomycin and derivatives, their production and their use as drugs |
| AU2010298338A1 (en) | 2009-09-22 | 2012-04-12 | Aileron Therapeutics, Inc. | Peptidomimetic macrocycles |
| EP2492344B1 (en) | 2009-10-22 | 2016-04-06 | PeptiDream Inc. | Rapid display method in translational synthesis of peptide |
| EP2646440A4 (en) | 2010-11-30 | 2014-06-18 | Univ Johns Hopkins | CYCLIC HYBRID LIBRARIES AND SCREENS FOR THIS |
| US9428845B1 (en) | 2010-12-28 | 2016-08-30 | Warp Drive Bio, Inc. | Identifying new therapeutic agents |
| WO2012174489A2 (en) | 2011-06-15 | 2012-12-20 | The Ohio State University | Small molecule composite surfaces as inhibitors of protein-protein interactions |
| PL3210627T3 (pl) | 2012-07-12 | 2023-04-17 | Hangzhou Dac Biotech Co., Ltd | Koniugaty zawierające cząsteczki wiążące się z komórką i środek cytotoksyczny |
| EP2922818B1 (en) | 2012-11-24 | 2018-09-05 | Hangzhou Dac Biotech Co., Ltd | Hydrophilic linkers and their uses for conjugation of drugs to cell binding molecules |
| EP2806274A1 (en) | 2013-05-24 | 2014-11-26 | AIT Austrian Institute of Technology GmbH | Lung cancer diagnostic method and means |
| US10233431B2 (en) | 2014-02-26 | 2019-03-19 | The Regents Of The University Of California | Producing 3-hydroxycarboxylic acid and ketone using polyketide synthases |
| CN106255882A (zh) | 2014-03-03 | 2016-12-21 | 耶路撒冷希伯来大学伊森姆研究发展公司 | 用于检测铜绿假单胞菌的方法和装置 |
| WO2018081592A2 (en) | 2016-10-28 | 2018-05-03 | Warp Drive Bio, Inc. | Compositions and methods for the production of compounds |
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- 2017-10-27 CN CN201780081023.1A patent/CN110506120A/zh active Pending
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- 2017-10-27 EP EP17865512.2A patent/EP3532633A4/en not_active Withdrawn
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| US20190249213A1 (en) | 2019-08-15 |
| EP3532633A2 (en) | 2019-09-04 |
| JP2020501519A (ja) | 2020-01-23 |
| WO2018081592A2 (en) | 2018-05-03 |
| AU2017350900A1 (en) | 2019-06-13 |
| EP3532633A4 (en) | 2020-09-09 |
| CN110506120A (zh) | 2019-11-26 |
| KR20190099396A (ko) | 2019-08-27 |
| US11479797B2 (en) | 2022-10-25 |
| WO2018081592A3 (en) | 2018-10-04 |
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