Literature summary for 2.3.1.B25 extracted from

Cohen, D.; Townsend, C.
A dual role for a polyketide synthase in dynemicin enediyne and anthraquinone biosynthesis (2018), Nat. Chem., 10, 231-236 .

Search for more literature for 2.3.1.B25

Cloned(Commentary)

Cloned (Comment)	Organism
gene pksE, DNA and amino acid sequence determination and analysis	Micromonospora chersina

Protein Variants

Protein Variants	Comment	Organism
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	Micromonospora chersina

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Micromonospora chersina	enzyme DynE8 makes 2, which is proposed to form the dynemicin enediyne and anthraquinone in the presence of accessory enzymes, and heptaene 1 in the presence of its native TE, DynE7. The end product is enediyne 3, synthesis pathway, overview	?	-	-
additional information	Micromonospora chersina NRRL B-24756	enzyme DynE8 makes 2, which is proposed to form the dynemicin enediyne and anthraquinone in the presence of accessory enzymes, and heptaene 1 in the presence of its native TE, DynE7. The end product is enediyne 3, synthesis pathway, overview	?	-	-

Organism

Organism	UniProt	Comment	Textmining
Micromonospora chersina	Q84HI8	-	-
Micromonospora chersina NRRL B-24756	Q84HI8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme DynE8 makes 2, which is proposed to form the dynemicin enediyne and anthraquinone in the presence of accessory enzymes, and heptaene 1 in the presence of its native TE, DynE7. The end product is enediyne 3, synthesis pathway, overview	Micromonospora chersina	?	-	-
additional information	enzyme DynE8 makes 2, which is proposed to form the dynemicin enediyne and anthraquinone in the presence of accessory enzymes, and heptaene 1 in the presence of its native TE, DynE7. The end product is enediyne 3, synthesis pathway, overview	Micromonospora chersina NRRL B-24756	?	-	-

Synonyms

Synonyms	Comment	Organism
DynE8	-	Micromonospora chersina
enediyne PKS	-	Micromonospora chersina
enediyne polyketide synthase	-	Micromonospora chersina
OKS	-	Micromonospora chersina
PksE	-	Micromonospora chersina
PksE	UniProt	Micromonospora chersina

General Information

General Information	Comment	Organism
metabolism	dual role for the octaketide synthase (OKS) in dynemicin enediyne and anthraquinone biosynthesis. An analysis of enediyne PKSs with their cognate thioesterases (TEs) from five different enediyne producers demonstrates production of heptaene 1 as their major product. Mixed-and-matched PKSs and TEs from 9- and 10-membered systems also produce 1, suggesting a convergent model of biosynthesis for this family of natural products. Despite the common production of 1 in enediyne systems, it is eliminated as a possible on-pathway precursor to the enediyne core. The calicheamicin enediyne PKS, CalE8, and the C-1027 TE are shown to make heptaene, but CalE8 is previously demonstrated to not restore antibiotic production in a C-1027 enediyne PKS knockout strain, leading to the conclusion that 1 is a shunt product of enediyne biosynthesis. The programmed product of the enediyne PKS is enzyme-bound beta-hydroxyhexaene 2	Micromonospora chersina
additional information	the enediyne antitumor antibiotics are a family of cytotoxic natural products distinguished by their 9- or 10-membered carbocyclic core structure containing a double bond flanked by two triple bonds	Micromonospora chersina
physiological function	the dynemicin enediyne PKS, DynE8, plays a dual role in the biosynthesis of both the enediyne and the anthraquinone halves of the molecule. DynE8 produces the core scaffolds of both the enediyne and anthraquinone	Micromonospora chersina

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)