Literature summary for 2.3.1.B25 extracted from

Frandsen, R.J.N.; Khorsand-Jamal, P.; Kongstad, K.T.; Nafisi, M.; Kannangara, R.M.; Staerk, D.; Okkels, F.T.; Binderup, K.; Madsen, B.; Moller, B.L.; Thrane, U.; Mortensen, U.H.
Heterologous production of the widely used natural food colorant carminic acid in Aspergillus nidulans (2018), Sci. Rep., 8, 12853 .

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Application

Application	Comment	Organism
synthesis	the enzyme OKS can be used in the heterologous production of the widely used natural food colorant carminic acid in Aspergillus nidulans, method, overview	Aloe arborescens

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of the gene encoding wild-type enzyme OKS in Aspergillus nidulans strain NID2252 controlled by the Aspergillus nidulans gpdA promoter as a single copy. Construction of a strain co-expressing OKS with ZhuI, which encodes the cyclases that catalyzes formation of the C7-C12 first ring closure. This strain shows 2.5, 2.2, and 2.1fold increases in flavokermesic acid, SEK4, and dehydro-SEK4 levels, respectively, compared to expression of OKS alone. This increase is 60% higher than what is observed with the strains expressing OKS in combination with either ZhuI (UniProt ID Q9F6D3) or ZhuJ (UniProt ID Q9F6D2), respectively, indicating that the cyclase and aromatase, in an additive manner, are able to increase the flux in the artificial de novo pathway towards the desired product, flavokermesic acid	Aloe arborescens

Cloned (Comment)

Organism

recombinant expression of the gene encoding wild-type enzyme OKS in Aspergillus nidulans strain NID2252 controlled by the Aspergillus nidulans gpdA promoter as a single copy. Construction of a strain co-expressing OKS with ZhuI, which encodes the cyclases that catalyzes formation of the C7-C12 first ring closure. This strain shows 2.5, 2.2, and 2.1fold increases in flavokermesic acid, SEK4, and dehydro-SEK4 levels, respectively, compared to expression of OKS alone. This increase is 60% higher than what is observed with the strains expressing OKS in combination with either ZhuI (UniProt ID Q9F6D3) or ZhuJ (UniProt ID Q9F6D2), respectively, indicating that the cyclase and aromatase, in an additive manner, are able to increase the flux in the artificial de novo pathway towards the desired product, flavokermesic acid

Aloe arborescens

Protein Variants

Protein Variants	Comment	Organism
additional information	formation of the tricyclic core of carminic acid is achieved via a two-step process wherein a plant type III polyketide synthase (PKS) forms a non-reduced linear octaketide, which subsequently is folded into the desired flavokermesic acid anthrone (FKA) structure by a cyclase and a aromatase from a bacterial type II PKS system. The formed FKA is oxidized to flavokermesic acid and kermesic acid, catalyzed by endogenous A. nidulans monooxygenases, and further converted to dcII and carminic acid by the Dactylopius coccus C-glucosyltransferase DcUGT2. The establishment of a functional biosynthetic carminic acid pathway in Aspergillus nidulans serves as an important step towards industrial-scale production of carminic acid via liquid-state fermentation using a microbial cell factory. Method optimization, overview. Deletion of the gene clusters that are responsible for formation of the major endogenous PKS products in Aspergillus nidulans improves the potential of Aspergillus nidulans as a cell factory for heterologous production of polyketides. Specifically, the gene clusters for production of asperthecin, onodictyphenone, and sterigmatocystin are eliminated as well as the genes responsible for green conidia pigment formation, wA and yA, were eliminated in a non-homologous endjoining defficient Aspergillus nidulans background. Besides the expected lack of conidial pigments, the resulting strain NID2252 does not display any visible effects on morphology and fitness	Aloe arborescens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
16 malonyl-CoA + 28 H+	Aloe arborescens	-	16 CoA + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one + 16 CO2 + 16 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Aloe arborescens	Q3L7F5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
16 malonyl-CoA + 28 H+	-	Aloe arborescens	16 CoA + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one + 16 CO2 + 16 H2O	-	?
additional information	the plant type III polyketide synthase, oktaketide synthase (OKS) forms a non-reduced linear octaketide	Aloe arborescens	?	-	-

Synonyms

Synonyms	Comment	Organism
plant type III OKS	-	Aloe arborescens
plant type III polyketide synthase	-	Aloe arborescens

General Information

General Information	Comment	Organism
metabolism	the enzyme OKS catalyzes the first step in carminic acid biosynthesis. Proposed biosynthetic pathway for formation of carminic acid and the required enzymatic steps. Formation of pathway intermediate flavokermesic acid anthrone can theoretically be achieved via either a one-step or two-step process, overview	Aloe arborescens