BG106478A - Ген на streptomyces avermitilis, модулиращ съотношението на авермектините в2:в1 - Google Patents

Ген на streptomyces avermitilis, модулиращ съотношението на авермектините в2:в1 Download PDF

Info

Publication number: BG106478A
Authority: BG; Bulgaria
Prior art keywords: avec; avermectins; amino acid; cells; avermitilis
Prior art date: 1999-08-12

Application number

BG106478A

Other languages

Bulgarian (bg)

English (en)

Inventor

Kim J. Stutzman-Engwall

Original Assignee

Pfizer Products 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.)

1999-08-12

Filing date

2002-03-05

Publication date

2004-02-27

2002-03-05 Application filed by Pfizer Products Inc. filed Critical Pfizer Products Inc.

2004-02-27 Publication of BG106478A publication Critical patent/BG106478A/bg

Links

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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
- 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
- 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
- C12N15/76—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Actinomyces; for Streptomyces
- 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
- C12N9/88—Lyases (4.)
- 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
- C12P17/181—Heterocyclic compounds containing oxygen atoms as the only ring heteroatoms in the condensed system, e.g. Salinomycin, Septamycin
- 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
- 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
- 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
- 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
- C12P19/623—Avermectin; Milbemycin; Ivermectin; C-076

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Chemical & Material Sciences (AREA)
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Bioinformatics & Cheminformatics (AREA)
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General Engineering & Computer Science (AREA)
Microbiology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Biomedical Technology (AREA)
Chemical Kinetics & Catalysis (AREA)
Molecular Biology (AREA)
General Chemical & Material Sciences (AREA)
Physics & Mathematics (AREA)
Plant Pathology (AREA)
Biophysics (AREA)
Medicinal Chemistry (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

BG106478A 1999-08-12 2002-03-05 Ген на streptomyces avermitilis, модулиращ съотношението на авермектините в2:в1 BG106478A (bg)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US09/372,934 US6248579B1 (en)	1998-02-13	1999-08-12	Streptomyces avermitilis gene directing the ratio of B2:B1 avermectins
PCT/IB2000/000996 WO2001012822A1 (en)	1999-08-12	2000-07-19	Streptomyces avermitilis gene directing the ratio of b2:b1 avermectins

Publications (1)

Publication Number	Publication Date
BG106478A true BG106478A (bg)	2004-02-27

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BG106478A BG106478A (bg)	1999-08-12	2002-03-05	Ген на streptomyces avermitilis, модулиращ съотношението на авермектините в2:в1

Country Status (37)

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US (8)	US6248579B1 (de)
EP (1)	EP1200605B1 (de)
JP (2)	JP3688640B2 (de)
KR (1)	KR100486006B1 (de)
CN (1)	CN1186447C (de)
AP (2)	AP2002002417A0 (de)
AR (1)	AR021450A1 (de)
AT (1)	ATE283363T1 (de)
AU (1)	AU779756B2 (de)
BG (1)	BG106478A (de)
BR (1)	BR0013093A (de)
CA (1)	CA2381427A1 (de)
CO (1)	CO5290296A1 (de)
CZ (1)	CZ2002297A3 (de)
DE (1)	DE60016231T2 (de)
EA (1)	EA004569B1 (de)
ES (1)	ES2231214T3 (de)
GT (2)	GT200000138A (de)
HK (1)	HK1046536B (de)
HR (1)	HRP20020131A2 (de)
HU (1)	HUP0202517A2 (de)
IL (1)	IL147562A0 (de)
IS (1)	IS6249A (de)
MA (1)	MA26811A1 (de)
MX (1)	MXPA02001514A (de)
NO (1)	NO20020665D0 (de)
OA (1)	OA11997A (de)
PA (1)	PA8499201A1 (de)
PE (1)	PE20010697A1 (de)
PL (1)	PL353770A1 (de)
PT (1)	PT1200605E (de)
SK (1)	SK1382002A3 (de)
TN (1)	TNSN00170A1 (de)
UY (1)	UY26287A1 (de)
WO (1)	WO2001012822A1 (de)
YU (1)	YU8402A (de)
ZA (1)	ZA200201071B (de)

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WO2001012821A1 (en) *	1999-08-12	2001-02-22	Pfizer Products Inc.	Streptomyces avermitilis gene directing the ratio of b2:b1 avermectins
ATE373644T1 (de)	2002-02-05	2007-10-15	Bristol Myers Squibb Co	N-substituierte 3-hydroxy-4-pyridinone und diese enthaltende pharmazeutika
RS50813B (sr) *	2002-02-12	2010-08-31	Pfizer Products Inc.	Streptomyces avermitilis gen koji određuje odnos b2:b1 avermektina
US7943160B2 (en) *	2002-05-09	2011-05-17	Scimetrics Limited Corp.	Pest control methods
US8440609B2 (en) *	2003-01-31	2013-05-14	Gerd Wallukat	Peptides against autoantibodies causing intolerance to cold and use thereof
KR100759130B1 (ko)	2005-02-12	2007-09-19	휴메드 주식회사	항 인테그린 항체 코팅스텐트 및 그의 제조방법
CN106148216B (zh)	2015-03-27	2019-06-04	浙江海正药业股份有限公司	一种链霉菌及其生产米尔贝霉素a3的方法

Family Cites Families (11)

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Publication number	Priority date	Publication date	Assignee	Title
US5525506A (en)	1987-01-23	1996-06-11	Pfizer Inc.	Process for production of avermectins and cultures therefor
US5234831A (en)	1987-01-23	1993-08-10	Pfizer Inc	Cultures for production of B avermectins
US5238848A (en)	1987-01-23	1993-08-24	Pfizer Inc	Cultures for production of avermectins
US5240850A (en)	1987-10-23	1993-08-31	Pfizer Inc.	Cultures for production of avermectin aglycones
ATE89604T1 (de)	1987-10-23	1993-06-15	Pfizer	Verfahren zur herstellung von aglykonen von avermectin und sie enthaltende kulturen.
DE69023036T2 (de)	1989-03-31	1996-06-13	Merck & Co Inc	Klonierung von Streptomyces avermitilis Genen zur Biosynthese von Avermectin und Verfahren zu ihrer Verwendung.
US5252474A (en)	1989-03-31	1993-10-12	Merck & Co., Inc.	Cloning genes from Streptomyces avermitilis for avermectin biosynthesis and the methods for their use
KR100221385B1 (ko)	1993-07-30	1999-10-01	디. 제이. 우드	스트렙토마이세스 아베르미틸리스로 부터의 측쇄 알파-케토산 데하이드로게나제 복합체를 암호화하는 유전자
CZ287404B6 (en) *	1993-10-05	2000-11-15	Pfizer	Process for preparing doramectin
FI942725A7 (fi)	1993-12-16	1995-06-17	Pfizer	Haaraketjuista alfaketohappodenydrogenaasikompleksia koodaavia geenejä Streptomyces avermitiliksesta
PL194270B1 (pl) *	1998-02-13	2007-05-31	Pfizer Prod Inc	Wyizolowana cząsteczka polinukleotydowa, cząsteczka oligonukleotydowa, zrekombinowany wektor, komórka gospodarza, wyizolowany produkt genu AveC S. avermitilis, wyizolowany produkt homologu genu AveC S. hygroscopicus, sposób wytwarzania zrekombinowanego produktu genu AveC, sposób wytwarzania zrekombinowanego produktu homologu genu AveC, cząsteczka polinukleotydowa, wektor do zastępowania genu, sposób identyfikowania mutacji otwartej ramki odczytuAveC, sposób wytwarzania nowych szczepów S. avermitilis, szczep S. avermitilis i sposób wytwarzaniaawermektyn

1999
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2000
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2001
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2002
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Also Published As

Publication number	Publication date
US6833263B2 (en)	2004-12-21
DE60016231T2 (de)	2005-12-08
US20010024818A1 (en)	2001-09-27
AP2002002417A0 (en)	2002-03-31
IL147562A0 (en)	2002-08-14
MXPA02001514A (es)	2002-07-02
US20010016350A1 (en)	2001-08-23
GT200000138A (es)	2002-02-02
DE60016231D1 (de)	2004-12-30
US7259241B2 (en)	2007-08-21
SK1382002A3 (en)	2002-11-06
PT1200605E (pt)	2005-04-29
KR100486006B1 (ko)	2005-05-03
CN1186447C (zh)	2005-01-26
JP2005198658A (ja)	2005-07-28
US7029887B2 (en)	2006-04-18
JP2003507018A (ja)	2003-02-25
EA004569B1 (ru)	2004-06-24
ZA200201071B (en)	2003-06-25
HUP0202517A2 (hu)	2002-11-28
UY26287A1 (es)	2001-03-16
CA2381427A1 (en)	2001-02-22
EA200200057A1 (ru)	2002-06-27
OA11997A (en)	2006-04-18
WO2001012822A1 (en)	2001-02-22
KR20020022809A (ko)	2002-03-27
HRP20020131A2 (en)	2003-12-31
US20030124607A1 (en)	2003-07-03
MA26811A1 (fr)	2004-12-20
NO20020665L (no)	2002-02-11
US20030129636A1 (en)	2003-07-10
AU5702100A (en)	2001-03-13
JP3688640B2 (ja)	2005-08-31
US20030134313A1 (en)	2003-07-17
HK1046536B (zh)	2005-05-13
US20050196777A1 (en)	2005-09-08
CN1370239A (zh)	2002-09-18
EP1200605B1 (de)	2004-11-24
GT200000138CA (es)	2002-02-02
HK1046536A1 (en)	2003-01-17
YU8402A (sh)	2006-03-03
AR021450A1 (es)	2002-07-17
IS6249A (is)	2002-01-25
CO5290296A1 (es)	2003-06-27
AU779756B2 (en)	2005-02-10
EP1200605A1 (de)	2002-05-02
CZ2002297A3 (cs)	2002-08-14
US20030129635A1 (en)	2003-07-10
NO20020665D0 (no)	2002-02-11
US6509159B2 (en)	2003-01-21
PL353770A1 (en)	2003-12-01
TNSN00170A1 (fr)	2005-11-10
ES2231214T3 (es)	2005-05-16
PE20010697A1 (es)	2001-07-05
US6248579B1 (en)	2001-06-19
PA8499201A1 (es)	2001-12-14
ATE283363T1 (de)	2004-12-15
US6511841B2 (en)	2003-01-28
BR0013093A (pt)	2002-08-13
AP2002002419A0 (en)	2002-03-31

Publication	Publication Date	Title
AU752343C (en)	2005-11-03	Streptomyces avermitilis gene directing the ratio of B2:B1 avermectins
EP1200605B1 (de)	2004-11-24	Streptomyces avermitilis gen zum regulieren des verhältnisses der b2:b1 avermectinen
EP1200606B1 (de)	2006-10-04	Streptomyces avermitilis gen zum regulieren des verhältnisses der b2:b1 avermectinen
ME00472B (me)	2011-10-10	Streptomyces avermitilis gen koji određuje odnos b2:b1 avermektina
MXPA00007915A (en)	2001-07-09	I(streptomyces avermitilis) gene directing the ratio of b2:b1 avermectins