EC Number   |
General Information |
Reference |
|---|
   2.3.1.B25 | evolution |
pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases |
722089 |
| 2.3.1.B25 | evolution |
pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases and grouped with other non-chalcone forming enzymes |
722034 |
| 2.3.1.B25 | 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 |
-, 757727 |
| 2.3.1.B25 | 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 |
758420 |
| 2.3.1.B25 | more |
active site structure of wild-type and mutant enzymes, overview. Amino acid residue at position 197 in the active site governs the chain length of the polyketide. Leucine at position 256 in the active site for both OKS and PCS influences the substrate preference for malonyl-CoA as a starting unit, while a glycine residue located in the same position and found in the catalytic pocket of chalcone synthase can possibly compel the enzyme to readily accept 4-coumaroyl-CoA as a starting unit |
722089 |
| 2.3.1.B25 | more |
the critical active-site residue 197, and the catalytic triad, Cys164, His303, and Asn336, are conserved in type III polyketide synthases, while the residues lining the active-site are exchanged to G197, L256, V338 (numbering in Madia sativa CHS). Active-site architecture of pentaketide chromone synthase compared to other type III polhaseyketide synt, crystal structure and hmology modeling, overview |
722034 |
| 2.3.1.B25 | more |
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 |
-, 757727 |
| 2.3.1.B25 | 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 |
-, 757727 |
| 2.3.1.B25 | physiological function |
the oktaketide synthase is involved in the biosynthesis of anthrones and anthraquinones in the medicinal plant |
722034 |
| 2.3.1.B25 | physiological function |
together with the C-glucosylated aloesone, aloesin, octaketide anthraquinones, such as aloe emodin occur naturally in Aloe arborescens and their in planta formation is thought to involve a ketoreductase or cyclases that utilize linear octaketides as substrates |
756452 |
