WO1995007979B1 - Synthesis of catechol from biomass-derived carbon sources - Google Patents
Synthesis of catechol from biomass-derived carbon sourcesInfo
- Publication number
- WO1995007979B1 WO1995007979B1 PCT/US1994/010382 US9410382W WO9507979B1 WO 1995007979 B1 WO1995007979 B1 WO 1995007979B1 US 9410382 W US9410382 W US 9410382W WO 9507979 B1 WO9507979 B1 WO 9507979B1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- genes encoding
- catechol
- carbon source
- dehydroshikimate
- synthase
- Prior art date
Links
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 title claims abstract 22
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 title claims abstract 11
- 229910052799 carbon Inorganic materials 0.000 title claims abstract 11
- 230000015572 biosynthetic process Effects 0.000 title claims abstract 6
- 239000002028 Biomass Substances 0.000 title claims abstract 3
- 238000003786 synthesis reaction Methods 0.000 title 1
- 108090000623 proteins and genes Proteins 0.000 claims abstract 15
- 241000588724 Escherichia coli Species 0.000 claims abstract 13
- 108010055053 3-dehydroshikimate dehydratase Proteins 0.000 claims abstract 11
- 108030003477 Protocatechuate decarboxylases Proteins 0.000 claims abstract 11
- 238000000034 method Methods 0.000 claims abstract 11
- 230000037361 pathway Effects 0.000 claims abstract 6
- 108050006180 3-dehydroquinate synthase Proteins 0.000 claims abstract 5
- SLWWJZMPHJJOPH-UHFFFAOYSA-N DHS Natural products OC1CC(C(O)=O)=CC(=O)C1O SLWWJZMPHJJOPH-UHFFFAOYSA-N 0.000 claims abstract 5
- 108050008280 Shikimate dehydrogenase Proteins 0.000 claims abstract 5
- YVYKOQWMJZXRRM-PUFIMZNGSA-N 3-dehydroshikimate Chemical compound O[C@@H]1C[C@H](C(O)=O)C=C(O)[C@@H]1O YVYKOQWMJZXRRM-PUFIMZNGSA-N 0.000 claims abstract 4
- -1 aromatic amino acid Chemical class 0.000 claims abstract 4
- 108010080376 3-Deoxy-7-Phosphoheptulonate Synthase Proteins 0.000 claims abstract 3
- 210000004027 cell Anatomy 0.000 claims 10
- 102000004190 Enzymes Human genes 0.000 claims 5
- 108090000790 Enzymes Proteins 0.000 claims 5
- 108020004511 Recombinant DNA Proteins 0.000 claims 5
- 238000012258 culturing Methods 0.000 claims 5
- 230000035772 mutation Effects 0.000 claims 5
- 239000013612 plasmid Substances 0.000 claims 5
- 229910019142 PO4 Inorganic materials 0.000 claims 4
- 102000014701 Transketolase Human genes 0.000 claims 4
- 108010043652 Transketolase Proteins 0.000 claims 4
- 238000004519 manufacturing process Methods 0.000 claims 4
- 239000010452 phosphate Substances 0.000 claims 4
- 241000894007 species Species 0.000 claims 4
- WTFXTQVDAKGDEY-UHFFFAOYSA-N (-)-chorismic acid Natural products OC1C=CC(C(O)=O)=CC1OC(=C)C(O)=O WTFXTQVDAKGDEY-UHFFFAOYSA-N 0.000 claims 3
- 241000588747 Klebsiella pneumoniae Species 0.000 claims 3
- 238000006243 chemical reaction Methods 0.000 claims 3
- WTFXTQVDAKGDEY-HTQZYQBOSA-N chorismic acid Chemical compound O[C@@H]1C=CC(C(O)=O)=C[C@H]1OC(=C)C(O)=O WTFXTQVDAKGDEY-HTQZYQBOSA-N 0.000 claims 3
- 241000894006 Bacteria Species 0.000 claims 2
- 125000002353 D-glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims 2
- WVMWZWGZRAXUBK-SYTVJDICSA-N 3-dehydroquinic acid Chemical compound O[C@@H]1C[C@](O)(C(O)=O)CC(=O)[C@H]1O WVMWZWGZRAXUBK-SYTVJDICSA-N 0.000 claims 1
- WVMWZWGZRAXUBK-UHFFFAOYSA-N 3-dehydroquinic acid Natural products OC1CC(O)(C(O)=O)CC(=O)C1O WVMWZWGZRAXUBK-UHFFFAOYSA-N 0.000 claims 1
- 101100163490 Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) aroA1 gene Proteins 0.000 claims 1
- 101150037081 aroA gene Proteins 0.000 claims 1
- 101150040872 aroE gene Proteins 0.000 claims 1
- 210000001236 prokaryotic cell Anatomy 0.000 claims 1
- 230000001131 transforming effect Effects 0.000 claims 1
- YQUVCSBJEUQKSH-UHFFFAOYSA-N 3,4-dihydroxybenzoic acid Chemical compound OC(=O)C1=CC=C(O)C(O)=C1 YQUVCSBJEUQKSH-UHFFFAOYSA-N 0.000 abstract 1
- 230000000911 decarboxylating effect Effects 0.000 abstract 1
- 230000002194 synthesizing effect Effects 0.000 abstract 1
Abstract
A method is provided for synthesizing catechol from a biomass-derived carbon source capable of being used by a host cell having a common pathway of aromatic amino acid biosynthesis. The method comprises the steps of biocatalytically converting the carbon source to 3-dehydroshikimate in said host cell, biocatalytically converting the DHS to protocatechuate, and decarboxylating the protocatechuate to form catechol. Also provided is a heterologue E. coli transformant characterized by the expression of genes encoding transhetolase, DAHP synthase, and DHQ synthase, further characterized by the constitutive expression of structural genes encoding 3-dehydroshikimate dehydratase and protocatechuate decarboxylase.
Claims
AMENDED CLAIMS
[received by the International Bureau on 3 March 1995 (03.03.95); original claims 11 and 14 amended; new claim 23 added; remaining claims unchanged (3 pages)]
6. The method of claim 5, wherein the host cell is E. coli strain AB2834.
7. The method of claim 6, wherein the host cell is transformed with plasmid pKD136. 8. A heterologous E . coli transformant characterized by the expression of additional structural genes encoding the enzyme species transketolase, 3-deoxy-D-arai»ino- heptulosonate 7-phosphate synthase, and 3-dehydroquinate ' synthase, and further characterized by the constitutive expression of structural genes encoding 3-dehydroshikimate dehydratase and protocatechuate decarboxylase.
9. The transformant of claim 8, wherein the structural genes encoding 3-dehydroshikimate dehydratase and protocatechuate decarboxylase are endogenous to Klebsiella pneumoniae .
10. The transformant of claim 8, wherein the E . coli strain is selected from the group of mutant cell lines consisting of mutations in the common pathway of aromatic amino acid biosynthesis that block conversion of 3- dehydroshikimate to chorismate.
11. A method for producing catechol biocatalyticaUy, said method comprising the step of culturing a heterologous E. coli transformant characterized by the constitutive expression of exogenous structural genes encoding the enzyme species transketolase, 3-deoxy-D-araJino- heptulosonate 7-phosphate synthase, 3-dehydroquinate synthase, 3-dehydroshikimate dehydratase and protocatechuate decarboxylase in the presence of a carbon source.
12. The method of claim 11, wherein the carbon source is D-glucose.
13. A method for producing catechol biocatalyticaUy, said method comprising the step of culturing a heterologous E. coli transformant characterized
by the constitutive expression of exogenous structural genes encoding the enzyme species transketolase, 3-deoxy-D- arabino-heptulosonate 7-phosphate synthase (DAHP synthase) , and 3-dehydroquinate synthase (DHQ synthase) , and 3- dehydroshikimate dehydratase and protocatechuate decarboxylase endogenous to Klebsiella pneumoniae in the presence of a carbon source.
14. A method for producing catechol biocatalyticaUy, said method comprising the step of culturing a prokaryotic cell, transformed with structural genes from Klebsiella pneumoniae which express the enzyme species 3-dehydroshikimate dehydratase and protocatechuate decarboxylase, in a medium containing a carbon source, under conditions in which the carbon source is converted to catechol at a rate greater than 0.21 millimoles/liter/hour.
15. A recombinantly transformed cell strain selected from the group consisting of E. coli strain AB2834/pKD136/p2-47, E. coli strain AB2834/pKD136/pKD8.243A, and E. coli strain AB2834/pKD136/pKD8.243B.
16. A method for producing catechol biocatalyticaUy, said method comprising the step of culturing a recombinantly transformed cell strain selected from the group consisting of E. coli strain AB2834/pKD136/p2-47, E. coli strain
AB2834/pKD136/pKD8.243A, and E. coli strain AB2834/pKD8.243B in the presence of a carbon source.
17. The method of claim 16, wherein the carbon source is D-glucose. 18. A heterologous mutant E. coli strain having an endogenous common pathway of aromatic amino acid biosynthesis and selected from the group consisting of strains having mutations in the common pathway that prevent conversion of 3-dehydroshikimate to chorismate, and further characterized by the constitutive expression of structural
genes encoding 3-dehydroshikimate dehydratase and protocatechuate decarboxylase.
19. The mutant cell line of claim 18, wherein the mutation is aroE. 20. A recombinant DNA construct comprising structural genes for 3-dehydroshikimate dehydratase and protocatechuate decarboxylase.
21. A recombinant DNA plasmid selected from the group consisting of plasmid p2-47, plasmid pKD8.243A, and plasmid pKD8.243B.
22. In a method for biosynthetic production of catechol in a host cell having an endogenous common pathway of aromatic amino acid biosynthesis, and a mutation in one of the genes encoding an enzyme of said pathway, wherein said mutation blocks the conversion of 3-dehydroshikimate to chorismate, and said host cell further characterized by the expression of structural genes encoding 3-deoxy-D- araJi-no-heptulosonate 7-phosphate synthase, 3- dehydroquinate synthase and transketolase, the improvement comprising transforming the host cell with recombinant DNA comprising consitutively expressed genes encoding 3- dehydroshikimate dehydratase and protocatechuate decarboxylase and culturing the transformed host cell in a medium containing a biomass-derived carbon source. 23. A heterologous prokaryote transformant having recombinant DNA sequences that express genes encoding 3- dehydroshikimate dehydratase and protocatechuate decarboxylase.
STATEMENT UNDER ARTICLE 19
Original claim 11 is amended to correct the spelling of 3-deoxy-D-αrαbz/zo- heptulosonate 7-phosphate synthase. Claim 14 is amended to specify the present invention produces catechol at a rate greater than 0.21 millimoles/liter/hour. Support for the amendment is found thoughout the specifiaction, and in particular at page 6, lines 16-20, page 13 lines 17-25, and page 22 lines 6-21 [ie, lOmM catechol/liter ÷ 48 hours = 0.21 mM/liter/hour]. New claim 23 is directed to prokaryote transformant having recombinant DNA sequences that express genes encoding 3-dehydroshikimate dehydratase and protocatechuate decarboxylase. Support for the amendment is found on page 8, lines 12-16. The abstract remains unchanged.
Priority Applications (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK94928589T DK0722488T3 (en) | 1994-09-14 | 1994-09-14 | Synthesis of chatechol from biomass-derived carbon sources |
| JP7509331A JPH09506242A (en) | 1993-09-16 | 1994-09-14 | Method for synthesizing catechol from biomass-derived carbon source |
| DE69433873T DE69433873T2 (en) | 1993-09-16 | 1994-09-14 | Synthesis of catechol by a biomass-derived carbon source |
| CA002171331A CA2171331C (en) | 1993-09-16 | 1994-09-14 | Synthesis of catechol from biomass-derived carbon sources |
| EP94928589A EP0722488B1 (en) | 1993-09-16 | 1994-09-14 | Synthesis of catechol from biomass-derived carbon sources |
| FI961233A FI115841B (en) | 1993-09-16 | 1996-03-15 | Synthesis of catechol from carbon sources derived from biomass |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/122,919 | 1993-09-16 | ||
| US08/122,919 US5629181A (en) | 1993-09-16 | 1993-09-16 | Synthesis of catechol from biomass-derived carbon sources |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| WO1995007979A1 WO1995007979A1 (en) | 1995-03-23 |
| WO1995007979B1 true WO1995007979B1 (en) | 1995-04-06 |
Family
ID=22405630
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/US1994/010382 WO1995007979A1 (en) | 1993-09-16 | 1994-09-14 | Synthesis of catechol from biomass-derived carbon sources |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US5629181A (en) |
| EP (1) | EP0722488B1 (en) |
| JP (1) | JPH09506242A (en) |
| CA (1) | CA2171331C (en) |
| DE (1) | DE69433873T2 (en) |
| ES (1) | ES2220916T3 (en) |
| FI (1) | FI115841B (en) |
| WO (1) | WO1995007979A1 (en) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0827542B1 (en) | 1995-05-05 | 2008-04-09 | Genencor International, Inc. | Application of glucose transport mutants for production of aromatic pathway compounds |
| US6043076A (en) | 1997-08-20 | 2000-03-28 | Board Of Regents Of University Of Nebraska | Gene encoding 2,3-dihydroxybenzoic acid decarboxylase |
| US6372461B1 (en) * | 1998-09-18 | 2002-04-16 | Board Of Directors Operating Michigan State University | Synthesis of vanillin from a carbon source |
| CA2366222A1 (en) * | 1999-03-23 | 2000-09-28 | Board Of Trustees Operating Michigan State University | Synthesis of 1,2,3,4-tetrahydroxybenzenes and 1,2,3-trihydroxybenzenes using myo-inositol-1-phosphate synthase and myo-inositol 2-dehydrogenase |
| US6472190B1 (en) * | 2000-03-16 | 2002-10-29 | Board Of Trustees Operating Michigan State Univerisity | Biocatalytic synthesis of galloid organics |
| US20060121581A1 (en) * | 2002-10-04 | 2006-06-08 | Cervin Marguerite A | Production of bacterial strains cross reference to related applications |
| US20050079617A1 (en) | 2003-10-03 | 2005-04-14 | Cervin Marguerite A. | Glucose transport mutants for production of biomaterial |
| WO2005030949A1 (en) * | 2003-09-24 | 2005-04-07 | Board Of Trustees Operating Michigan State University | Methods and materials for the production of shikimic acid |
| DK2447356T3 (en) | 2005-06-07 | 2016-06-06 | Dsm Nutritional Products Ag | Eukaryotic MICROORGANISMS FOR PRODUCTION OF LIPIDS AND ANTIOXIDANTS |
| CA2659603C (en) * | 2006-08-01 | 2017-03-07 | Ocean Nutrition Canada Limited | Oil producing microbes and methods of modification thereof |
| US8415496B2 (en) | 2009-06-16 | 2013-04-09 | Amyris, Inc. | Biobased polyesters |
| WO2010148080A2 (en) | 2009-06-16 | 2010-12-23 | Draths Corporation | Cyclohexane 1,4 carboxylates |
| CN102725258A (en) | 2009-06-16 | 2012-10-10 | 阿迈瑞斯公司 | Cyclohexane-1,4-dicarboxylates |
| WO2010148049A2 (en) | 2009-06-16 | 2010-12-23 | Draths Corporation | Preparation of trans, trans muconic acid and trans, trans muconates |
| WO2010148063A2 (en) | 2009-06-16 | 2010-12-23 | Draths Corporation | Cyclohexene 1,4-carboxylates |
| WO2011022588A1 (en) * | 2009-08-21 | 2011-02-24 | Draths Corporation | Sulfonation of polyhydroxyaromatics |
| CN103667166A (en) * | 2012-09-21 | 2014-03-26 | 天津工业生物技术研究所 | Escherichia coli for producing adipic acid precursor namely cis,cis-muconic acid and application of escherichia coli |
| DK2970926T3 (en) | 2013-03-13 | 2018-04-16 | Dsm Nutritional Products Ag | GENMANIPULATION OF MICROorganisms |
| WO2016036915A1 (en) * | 2014-09-03 | 2016-03-10 | Coffa Gianguido | Genetically modified microbes for the biological conversion of carbonaceous materials to protocatechuic acid |
| AR104042A1 (en) | 2015-03-26 | 2017-06-21 | Mara Renewables Corp | HIGH-DENSITY PRODUCTION OF BIOMASS AND OIL USING GLUCEROL IN GROSS |
| CN107849514A (en) | 2015-07-13 | 2018-03-27 | 玛拉可再生能源公司 | Strengthen the microalgae metabolism of xylose |
| US10961526B2 (en) | 2016-03-28 | 2021-03-30 | Research Institute Of Innovative Technology For The Earth | Transformant, and method for producing protocatechuic acid or salt thereof using same |
| US10851395B2 (en) | 2016-06-10 | 2020-12-01 | MARA Renewables Corporation | Method of making lipids with improved cold flow properties |
| US11359217B2 (en) | 2018-05-01 | 2022-06-14 | Research Institute Of Innovative Technology For The Earth | Transformant of coryneform bacterium and production method for useful compound using same |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH616706A5 (en) * | 1973-11-23 | 1980-04-15 | Takeda Chemical Industries Ltd | |
| DE3128411A1 (en) * | 1980-07-18 | 1983-09-15 | Unisearch Ltd., 2033 Kensington, New South Wales | CULTURAL MUTANT OF ESCCHERICHIA COLI AND METHOD FOR THE PRODUCTION OF PHENYLALANINE |
| JPH0732710B2 (en) * | 1983-05-28 | 1995-04-12 | 協和醗酵工業株式会社 | Method for producing phenylalanine |
| JPS6178378A (en) * | 1984-09-27 | 1986-04-21 | Ajinomoto Co Inc | Coryne-type bacteria having recombinant dna, and production of aromatic amino acid using same |
| US4753883A (en) * | 1986-05-07 | 1988-06-28 | Biotechnica International, Inc. | Enzyme deregulation |
| US5168056A (en) * | 1991-02-08 | 1992-12-01 | Purdue Research Foundation | Enhanced production of common aromatic pathway compounds |
| US5272073A (en) * | 1992-06-30 | 1993-12-21 | Purdue Research Foundation | Biocatalytic synthesis of catechol from glucose |
-
1993
- 1993-09-16 US US08/122,919 patent/US5629181A/en not_active Expired - Lifetime
-
1994
- 1994-09-14 JP JP7509331A patent/JPH09506242A/en not_active Withdrawn
- 1994-09-14 ES ES94928589T patent/ES2220916T3/en not_active Expired - Lifetime
- 1994-09-14 EP EP94928589A patent/EP0722488B1/en not_active Expired - Lifetime
- 1994-09-14 DE DE69433873T patent/DE69433873T2/en not_active Expired - Lifetime
- 1994-09-14 CA CA002171331A patent/CA2171331C/en not_active Expired - Lifetime
- 1994-09-14 WO PCT/US1994/010382 patent/WO1995007979A1/en active IP Right Grant
-
1996
- 1996-03-15 FI FI961233A patent/FI115841B/en not_active IP Right Cessation
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| WO1995007979B1 (en) | Synthesis of catechol from biomass-derived carbon sources | |
| US5272073A (en) | Biocatalytic synthesis of catechol from glucose | |
| US5616496A (en) | Bacterial cell tranformants for production of cis, cis-muconic acid and catechol | |
| US5168056A (en) | Enhanced production of common aromatic pathway compounds | |
| CA2124214C (en) | Materials and methods for biosynthesis of serine and serine-related products | |
| CA2171331C (en) | Synthesis of catechol from biomass-derived carbon sources | |
| CA2262813A1 (en) | Novel strains of escherichia coli, methods of preparing the same and use thereof in fermentation processes for l-threonine production | |
| WO1996008567B1 (en) | Microorganisms and methods for overproduction of dahp by cloned pps gene | |
| CN104379729A (en) | Useful microorganism, and method for producing desired substance | |
| Jäger et al. | A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins | |
| KR100528527B1 (en) | Microbial preparation of substances from aromatic metabolism/i | |
| CA2890922A1 (en) | Method for producing phenol from renewable resources by fermentation | |
| JP7646119B2 (en) | Genetically modified microorganisms for producing 3-hydroxyadipic acid, α-hydromuconic acid and/or adipic acid and methods for producing said chemicals | |
| EP0736604A2 (en) | Materials and methods for the production of D-phenylalanine | |
| US11932896B2 (en) | Host cells and methods for producing hydroxytyrosol | |
| KR20080077253A (en) | RMNA stabilization method | |
| Sanz et al. | Genetic characterization of the cyclohexane carboxylate degradation pathway in the denitrifying bacterium Aromatoleum sp. CIB | |
| US5304475A (en) | Method for production of L-phenylalanine by recombinant E. coli | |
| US20230407351A1 (en) | Recombinant host cells to produce anthranilic acid | |
| EP0183006B1 (en) | A recombinant dna-molecule, coryneform bacteria carrying recombinant dna and process for producing an aromatic amino acid by using the same | |
| US6156545A (en) | Biosynthesis method enabling the preparation of cobalamins | |
| KR20110135261A (en) | Recombinant microorganism having butanol producing ability and method for producing butanol using same | |
| CN113493760B (en) | Corynebacterium glutamicum for biosynthesis of 2-phenethyl alcohol, construction method and application | |
| KR101697368B1 (en) | Enhanced Butanol Producing Recombinant Microorganisms and Method for Preparing Butanol Using the Same | |
| Frost et al. | Synthesis of adipic acid from biomass-derived carbon sources |