2.3.1.B25: octaketide synthase
This is an abbreviated version!
For detailed information about octaketide synthase, go to the full flat file.
Word Map on EC 2.3.1.B25
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2.3.1.B25
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plant-specific
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aloe
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arborescens
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condensations
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pentaketide
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chromone
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anthraquinone
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dynemicins
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micromonospora
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10-membered
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benzophenone
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calicheamicin
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hexaketide
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precursor-directed
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anthrone
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naphthopyrone
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benzalacetone
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nonaketide
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n-methylanthraniloyl-coa
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acridone
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spring-8
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palmatum
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tetraketides
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neocarzinostatin
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synthesis
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molecular biology
- 2.3.1.B25
-
plant-specific
- aloe
- arborescens
-
condensations
-
pentaketide
- chromone
- anthraquinone
- dynemicins
- micromonospora
-
10-membered
- benzophenone
-
calicheamicin
-
hexaketide
-
precursor-directed
- anthrone
-
naphthopyrone
- benzalacetone
-
nonaketide
- n-methylanthraniloyl-coa
-
acridone
-
spring-8
- palmatum
-
tetraketides
-
neocarzinostatin
- synthesis
- molecular biology
Reaction
16 malonyl-CoA
+
28 H+
=
16 CoA
+
Synonyms
AaOKS, DynE8, enediyne PKS, enediyne polyketide synthase, OKS, oktaketide synthase, PksE, plant type III OKS, plant type III polyketide synthase
ECTree
2.3.1.B25 octaketide synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.B25 - octaketide synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G197A
site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing heptaketides
G197T
site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing hexaketides
G197W
site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing tri- and pentaketides
G207A
site-directed mutagenesis, the G207A mutant loses the octaketide-forming activity and yields the heptaketide aloesone in addition to 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
G207F
site-directed mutagenesis, the bulky substitution G207F mutant loses the octaketide-forming activity and yields the pentaketide 2,7-dihydroxy-5-methylchromone
G207L
site-directed mutagenesis, the bulky substitution G207F mutant loses the octaketide-forming activity and yields the pentaketide 2,7-dihydroxy-5-methylchromone
G207M
site-directed mutagenesis, OKS G207M mutant completely loses the octaketide-forming activity, but efficiently produces an unnatural pentaketide, 2,7-dihydroxy-5-methylchromone, from five molecules of malonyl-CoA, not a 5,7-diydroxy-5-methylchromne like the pentaketide chromone synthase, EC 2.3.1.216
G207T
site-directed mutagenesis, the G207T mutant loses the octaketide-forming activity and yields a hexaketide, 6-(2,4-dihydroxy-6-methylphenyl)-4-methoxy-2-pyrone, from six molecules of malonyl-CoA
G207W
site-directed mutagenesis, the mutant loses the octaketide-forming activity and yields a tetraketide, tetracetic acid lactone, along with the triketide, triacetic acid lactone, without the formation of an aromatic ring system
additional information
additional information
generation molecularly diverse plant type III polyketides through rational engineering of the oktaketide synthase active site
additional information
oktaketide synthase, EC 2.3.1.OKS, and pentaketide chromone synthase, EC 2.3.1.216, are not functionally interconvertible by the single amino acid switch at residue 207
additional information
biosynthesis of the C-glucosylated anthraquinone, dcII, a precursor for carminic acid, using a combination of enzymes derived from Aloe arborescens, Streptomyces sp. R1128, and the insect Dactylopius coccus. The pathway, which consists of AaOKS, StZhuI, StZhuJ, and DcUGT2, presents an alternative biosynthetic approach for the production of polyketides by using a type III polyketide synthase (PKS) and tailoring enzymes originating from a type II PKS system. Transient expression in Nicotiana benthamiana. Method, detailed overview
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
additional information
individual inactivation of all potential PKS-encoding genes using CRISPR-Cas9 method, the knockouts fail to identify the anthraquinone PKS, identification of dynemicin enediyne PKS, DynE8
additional information
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individual inactivation of all potential PKS-encoding genes using CRISPR-Cas9 method, the knockouts fail to identify the anthraquinone PKS, identification of dynemicin enediyne PKS, DynE8
additional information
Micromonospora chersina NRRL B-24756
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individual inactivation of all potential PKS-encoding genes using CRISPR-Cas9 method, the knockouts fail to identify the anthraquinone PKS, identification of dynemicin enediyne PKS, DynE8
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