WO2013023999A1 - Carboxylation régiosélective de composés de substrats non naturels par l'utilisation de décarboxylases - Google Patents

Carboxylation régiosélective de composés de substrats non naturels par l'utilisation de décarboxylases Download PDF

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Publication number
WO2013023999A1
WO2013023999A1 PCT/EP2012/065628 EP2012065628W WO2013023999A1 WO 2013023999 A1 WO2013023999 A1 WO 2013023999A1 EP 2012065628 W EP2012065628 W EP 2012065628W WO 2013023999 A1 WO2013023999 A1 WO 2013023999A1
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Prior art keywords
carboxylation
substrate
decarboxylase
dhbd
process according
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PCT/EP2012/065628
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English (en)
Inventor
Kurt Faber
Silvia M. GLUECK
Christiane WUENSCH
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Acib Gmbh
Karl-Franzens Universität Graz
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Publication of WO2013023999A1 publication Critical patent/WO2013023999A1/fr

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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
    • C12N9/88—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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
    • C12P7/42—Hydroxy-carboxylic acids
    • 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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
    • C12P7/44—Polycarboxylic acids

Definitions

  • the present invention relates to the regioselective carboxylation of nonnatural substrate compounds using a decarboxylase.
  • carboxylation reactions are mediated by the cofactor biotin, whereas photosynthesis depends on Mg 2+ -dependent RuBisCO. These reactions are high-energy demanding (13, 14) ⁇ and require ATP for the fixation of CO 2 onto biotin, which serves as activated C0 2 -derivative for the carboxylation of Acyl- CoA (15).
  • reductive carboxylation e.g. pyruvate + C0 2 yielding malate
  • NADPH NADPH
  • biodegradation In contrast to highly directed biosynthetic carboxylation pathways, several unspecific C0 2 -fixation reactions occur in catabolic (biodegradation) pathways.
  • the prime goal of biodegradation is making toxic compounds more hydrophilic, thereby enhancing their solubility in water in order to reduce their affinity for sensitive lipophilic biological components, such as membranes, proteins, etc.
  • catabolic enzymes In order to make these processes more efficient, catabolic enzymes usually possess relaxed substrate specificities and are able to act on a large variety of substrates. Carboxylases involved in biodegradation have been exploited to an astonishingly limited extent for preparative biotransformations (16, 17, 18).
  • Carboxylation reactions are important biosynthetic processes, the enzymes involved are usually highly substrate-specific and consequently it was rather surprising, that nonnatural (man-made) substrates have been carboxylated at reasonable rates.
  • the present invention relates to a process for the regioselective carboxylation of nonnatural substrate compounds using a decarboxylase.
  • One aspect of the invention relates to such a process, wherein the
  • carboxylation is an o- or ⁇ -carboxylation.
  • a further aspect of the invention relates to such a process, wherein at least
  • 25% of the nonnatural substrate are converted, preferably at least 30%.
  • a further aspect of the invention relates to such a process, wherein the decarboxylase is selected from the group consisting of dihydroxybenzoic acid decarboxylase (DHBD), dihydroxyphthaiic acid decarboxylase (DHPD), salicylic acid decarboxylase (SAD), pyruvate decarboxylase (PDC), phenolic acid decarboxylase (PAD), and ferulic acid decarboxylase (FDC).
  • DHBD dihydroxybenzoic acid decarboxylase
  • DHPD dihydroxyphthaiic acid decarboxylase
  • SAD salicylic acid decarboxylase
  • PDC pyruvate decarboxylase
  • PAD phenolic acid decarboxylase
  • FDC ferulic acid decarboxylase
  • a further aspect of the invention relates to such a process, wherein the nonnatural substrate is compound of formula I,
  • A is a mono- or bicyclic aromatic or heteroaromatic ring
  • each R1 is independently from one another selected from the group consisting of halogen, carboxy, -(CH 2 ) n OH, -NH 2 , Ci. 3 alkoxy, Ci. 3 alkyl, d. 3 alkenyl, and
  • n 0, 1 , 2, 3 or 4.
  • a further aspect of the invention relates to such a process, wherein the nonnatural substrate is hydroxystyrene.
  • a further aspect of the invention relates to a process for the regioselective carboxylation of natural and nonnatural substrate compounds, wherein an organic cosolvent is added in order to enhance the solubility of the substrate and/or product(s) and to increase the conversion.
  • a further aspect of the invention relates to such process, wherein the organic cosolvent is selected from the group consisting of D SO, DMF, EtOH, acetone, acetonitrile, A/-methyl-2-pyrrolidone, glycerin, formamide, and 1 ,4-dioxane.
  • the organic cosolvent is selected from the group consisting of D SO, DMF, EtOH, acetone, acetonitrile, A/-methyl-2-pyrrolidone, glycerin, formamide, and 1 ,4-dioxane.
  • a further aspect of the invention relates to a process for manufacturing a carboxylated compound, comprising the steps of:
  • a further aspect of the invention relates to such process, wherein said carbon source is C0 2 or a carbonate buffer.
  • a further aspect of the invention relates to a compound obtained in such processes for use in pharmaceutical, cosmetic and/or food industry.
  • Enzymes allow many chemical reactions to occur within the homeostasis constraints of a living system.
  • Enzymes function as organic catalysts.
  • the non-natural substrate relates to a substrate which is not known to be natural to the respective enzyme.
  • mono- or bicyclic aromatic or heteroaromatic ring refers to a mono- or bicyclic aromatic or heteroaromatic ring system comprising 5 to 10 ring atoms selected from C, N, O and S.
  • aromatic or heteroaromatic mono- or bicyclic ring systems include but are not limited to phenyl, pyridyl, pyrrolyl, pyrrazolyl, napthyl, quinolinyl, isoquinolinyl, tetrahydroisoquinyl, indolyl, indazolyl, benzimidazolyl, benzthiadiazolyl and imidazopyridinyl.
  • halogen refers to F, CI, Br and I.
  • Fig. 1 Carboxylation reaction of resorcinol using 2,6-DHBD Rsp applying various organic cosolvents categorized in four groups
  • Fig. 2 Carboxylation of catechol applying SAD Tm in presence of selected water-miscible organic cosolvents at concentrations of 0% - 50% (v/v)
  • Fig. 3 Carboxylation reaction of resorcinol applying 2,6-DHBD Rsp using various bicarbonate salts;
  • IL ionic liquid (1 -butyl-3-methylimidazolium hydrogen carbonate solution -50% in methanol/water 2/3; 200 ⁇ _)
  • Fig. 4 Substrate concentration study of the carboxylation of resorcinol employing 2,6-DHBD Rsp as biocatalyst
  • Fig. 5 Carboxylation reaction of resorcinol applying 2,6-DHBD Rsp at different temperatures
  • Fig. 6 Carboxylation reaction of resorcinol applying 2,6-DHBD Rsp at 10°C and different pH values.
  • Fig 7 Cosolvent study for the carboxylation of resorcinol and catechol applying 2,6-DHBD Rsp and SAD Tm as biocatalyst
  • the genes were synthesized at geneart (Germany, Regensburg) and subcloned in a common pET vector (pET 21 a). The obtained plasmid was
  • the cells were disrupted using ultrasonication and the separated supernatant and remaining pellet were analyzed by SDS-page.
  • the decarboxylases of the Aspergillus and Bordetella strain were nicely soluble whereas in case of the Comamonas strain the protein was mostly insoluble and remained in the pellet and in case of the protein of the
  • 2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus oryzae (2,3- DHBD Ao)
  • salicylic acid decarboxylase from Trichosporon moniliiforme SAD Tm
  • 2,6-dihydroxybenzoic acid decarboxylase from Rhizobium sp. (2,6-DHBD Rsp) were synthesized and ligated into a pET 21 a (+) vector at Geneart AG (Germany, Regensburg).
  • the obtained plasmids were transformed in a standard E. coli host [BL21 (DE3)] using IPTG-induction for overexpression.
  • Phenolic acid decarboxylases from Lactobacillus plantarum (PAD Lp) and from Bacillus amyloliquefaciens (PAD Ba) subcloned in a pET 28a (+) vector were kindly provided by Byung-Gee Kim (School of Chemical and Biological Engineering, Institute of Bioengineering, Seoul National University). The plasmids were
  • Phenolic acid decarboxylases from Mycobacterium colombiense (PAD Mc), Methylobacterium sp. (PAD Msp), Pantoea sp. (PAD Psp), Lactoccocus lactis (PAD LI), and ferulic acid decarboxylase from Enterobacter sp. (FDC Esp) were synthesized at geneart AG (Germany, Regensburg) and subcloned in a common pET vector [pET 21 a (+)]. The obtained plasmids were transformed in a standard E. coli host [BL21 (DE3)] using IPTG-induction for overexpression.
  • heterologous overexpression of all enzymes was performed as follows: For preculturing 500 ml_ LB medium [Trypton (10 g/L), yeast extract (5 g/L), NaCI (5 g/L)] supplemented with the appropriate antibiotics [ampicillin (100 ⁇ g/mL) for 2,3- DHBD Ao, SAD Tm, 2,6-DHBD Rsp, PAD Mc, PAD Msp, PAD Psp.
  • PAD LI and FDC Esp; kanamycin (50 ⁇ g/mL) for PAD Lp and PAD Ba] were inoculated with 3 mL ONC (starter culture) and incubated at 37°C and 120 rpm until an OD 60 o of 0.6- 1 .0 was reached. Then IPTG [450 ⁇ g/mL, 2 mM (for 2,3-DHBD Ao) or 175 ⁇ g/mL, 0.5 mM (for all other decarboxylases)] was added for induction and the cells left overnight at 20 °C and 120 rpm. The next day the cells were harvested by
  • Table 1 Summary of all overexpressed enzymes and wild-type organisms applied for the o- and -carboxylation.
  • PADJV!sp Phenolic acid decarboxylase Methylobacterium sp.
  • FCC Fab-Crew-Collection, in-house strain collection
  • PAD_Ba a 18° 26° 5 34 ' 10 : 6° 20
  • lyophilized whole cells (30mg) resuspended in phosphate buffer (1 ml_, pH 7.0, 100 mM) or a cell suspension obtained after cell disruption of lyophilized or freshly harvested cells using ultrasonication (1 ml_, supernatant and pellet) was used.
  • the substrate was added as a stock solution (10 - 20 ⁇ _) to a final concentration of 10 mM. The mixture was shaken at 30 °C and
  • 4,5-DHPA 4,5-dihydroxyphthalic acid
  • 2,3-DHBA 2,3-dihydroxybenzoic acid
  • the natural substrate was used for the screening of the carboxylation activity.
  • the natural substrate is catechol which is supposed to be carboxylated regioselective in o/ !0-position to the OH-group yielding the corresponding 2,3-dihydroxybenzoic acid.
  • the natural substrate is 3,4-dihydroxybenzoic acid obtaining 4,5-dihydroxyphthalic acid as expected product.
  • bicarbonate was added to the biotransformation which generated a certain C0 2 pressure in the tightly closed reaction vessel.
  • Lyophilized whole cells (30 mg E. coli host cells containing the corresponding overexpressed enzyme or whole wild-type microbial cells) were resuspended in phosphate buffer (1 ml_ or 900 ⁇ _, pH 5.5, 100 mM) and rehydrated for 30min.
  • the substrate was added either directly or as a stock solution (1 0 - 1 00 ⁇ _) to yield a final concentration of 1 0 mM, followed by addition of KHC0 3 (0.1 - 3M, 1 0 - 300 mg).
  • KHC0 3 0.1 - 3M, 1 0 - 300 mg.
  • all screenings were performed with and without the addition of organic cosolvent (20% v/v acetonitrile).
  • the substrate stock solution was prepared in acetonitrile to overcome solubility problems, leading to a final acetonitrile concentration of 10% v/v in the reaction mixture.
  • the substrate stock solution was prepared in acetonitrile to overcome solubility problems, leading to a final acetonitrile concentration of 1 % v/v in the reaction mixture. The work up was performed as described above.
  • a carboxylation activity of 5% was detected towards the natural substrate 3,4-DHBA.
  • the 2.3-DHBD accepted resorcin as a substrate yielding 2,6-dihydroxybenzoic acid as the expected product (conv. 15%, Table 7).
  • Catechol was converted in a low to moderate rate of the 4,5-DHPD from B. pertussis and C. testosteroni obtaining 2,3- DHBA as the expected products (conv. 5% and 25%, Table 7).
  • phenol and pyrrol as substrate for none of the enzymes a carboxylation activity was detected.
  • testosteroni Example 5 Conditions - carboxylation process
  • DTT Dithiothreitol
  • the standard substrate concentration used in these experiments was 10 mM, however by applying a 10fold increase of the substrate concentration (100 mM) an equally good conversion was obtained.
  • Lyophilized whole cells [30mg, either wild-type microorganisms (preparation B) or E. coli host cells containing the corresponding overexpressed enzyme (preparation A)] were resuspended in phosphate buffer (900 ⁇ _, pH 5.5, 100 mM) and were re h yd rated for 30 min.
  • the substrate was added as a stock solution (100 ⁇ _) to yield a final con- centration of 10 mM, followed by addition of KHC0 3 (3M, 300 mg). After the addition of bicarbonate the vials were immediately tightly closed and the mixture was shaken at 30 °C and 120 rpm.
  • PAD A 35 ° 0 0 0 0 plantarum
  • PAD A 35 ° 0 0 0 0 amyloliquefaciens
  • Preparation B whole wild-type microbial cells

Abstract

La présente invention concerne la carboxylation régiosélective de composés de substrats non naturels par l'utilisation d'une décarboxylase.
PCT/EP2012/065628 2011-08-12 2012-08-09 Carboxylation régiosélective de composés de substrats non naturels par l'utilisation de décarboxylases WO2013023999A1 (fr)

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US201161523226P 2011-08-12 2011-08-12
US61/523,226 2011-08-12
EP11177386 2011-08-12
EP11177386.7 2011-08-12

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Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2017111598A1 (fr) 2015-12-22 2017-06-29 Nederlandse Organisatie Voor Toegepast-Natuurwetenschappelijk Onderzoek Tno Procédé de préparation de composés phényles
CN108715826A (zh) * 2018-05-25 2018-10-30 上海交通大学 一种不依赖辅因子的全细胞催化合成芳香化合物的方法
CN110205316A (zh) * 2019-06-21 2019-09-06 济宁学院 一种酶法降解4-氨基水杨酸的方法
CN110241102A (zh) * 2019-06-21 2019-09-17 济宁学院 一种酶法降解2,6-二羟基苯甲酸的方法
CN112266881A (zh) * 2020-10-20 2021-01-26 山东农业大学 一株解淀粉芽胞杆菌及其在防治苹果重茬障碍中的应用
WO2021198888A1 (fr) 2020-03-31 2021-10-07 Pi Industries Ltd. Réaction de carboxylation catalysée par une enzyme améliorée
CN113846131A (zh) * 2020-06-28 2021-12-28 尚科生物医药（上海）有限公司 一种制备(r)-3-氨基-4-(2,4,5-三氟苯基)-丁酸的方法
US11957545B2 (en) 2017-09-26 2024-04-16 Smith & Nephew Plc Sensor positioning and optical sensing for sensor enabled wound therapy dressings and systems

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Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2017111598A1 (fr) 2015-12-22 2017-06-29 Nederlandse Organisatie Voor Toegepast-Natuurwetenschappelijk Onderzoek Tno Procédé de préparation de composés phényles
US11957545B2 (en) 2017-09-26 2024-04-16 Smith & Nephew Plc Sensor positioning and optical sensing for sensor enabled wound therapy dressings and systems
CN108715826A (zh) * 2018-05-25 2018-10-30 上海交通大学 一种不依赖辅因子的全细胞催化合成芳香化合物的方法
CN108715826B (zh) * 2018-05-25 2021-12-10 上海交通大学 一种不依赖辅因子的全细胞催化合成芳香化合物的方法
CN110205316A (zh) * 2019-06-21 2019-09-06 济宁学院 一种酶法降解4-氨基水杨酸的方法
CN110241102A (zh) * 2019-06-21 2019-09-17 济宁学院 一种酶法降解2,6-二羟基苯甲酸的方法
WO2021198888A1 (fr) 2020-03-31 2021-10-07 Pi Industries Ltd. Réaction de carboxylation catalysée par une enzyme améliorée
CN113846131A (zh) * 2020-06-28 2021-12-28 尚科生物医药（上海）有限公司 一种制备(r)-3-氨基-4-(2,4,5-三氟苯基)-丁酸的方法
CN112266881A (zh) * 2020-10-20 2021-01-26 山东农业大学 一株解淀粉芽胞杆菌及其在防治苹果重茬障碍中的应用
CN112266881B (zh) * 2020-10-20 2021-11-19 山东农业大学 一株解淀粉芽胞杆菌及其在防治苹果重茬障碍中的应用

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