Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin
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Cited by (109)
Synthetic biology approaches for secondary metabolism engineering
2021, Microbial Cell Factories Engineering for Production of BiomoleculesBiosynthesis of pyranonaphthoquinone polyketides reveals diverse strategies for enzymatic carbon-carbon bond formation
2013, Current Opinion in Chemical BiologyCitation Excerpt :One distinct subclass of aromatic polyketides is the pyranonaphthoquinones, which have a fused three-ring structure composed of a pyran, a quinone and a benzene ring (Figure 1). The p-quinone is typically found as the central ring, like in actinorhodin, granaticin, medermycin and frenolicin, but in the case of alnumycin A the quinone structure has an atypical position as a lateral ring [2–6]. The remarkable feature of pyranonaphthoquinones is the wealth of non-canonical modifications made to the core aglycone units, which are in many cases accomplished via CC bonds.
Ketosynthase III as a gateway to engineering the biosynthesis of antitumoral benastatin derivatives
2009, Journal of BiotechnologyChapter 16 In Vitro Analysis of Type II Polyketide Synthase
2009, Methods in EnzymologyCitation Excerpt :Most type II PKSs are primed by an acetate unit with acetyl‐ACP or through the decarboxylation of a malonyl‐ACP. Numerous medicinally important polyketides are initiated with nonacetate starter units (Fig. 16.1), including daunorubicin (propionate) (Bao et al., 1999), tetracycline (malonamate) (Zhang et al., 2006), frenolicin (butyrate) (Bibb et al., 1994), R1128 (medium‐length alkylacyl groups) (Tang et al., 2004b), enterocin (benzoate) (Cheng et al., 2007), and hedamycin (a reduced polyketide starter unit) (Bililign et al., 2004). Genetic characterizations of the corresponding gene clusters has revealed the presence of various enzymes that can synthesize the starter unit, bypass the acetate priming, and transfer the starter unit to the minimal PKS.
Proposed Arrangement of Proteins Forming a Bacterial Type II Polyketide Synthase
2008, Chemistry and BiologyCitation Excerpt :The enzyme encoded by dpsC is a homolog of the β-ketoacyl: ACP synthase III (KASIII) responsible for the condensation between the starter unit and the first extender unit, while dpsD encodes a proposed MCAT (Rajgarhia and Strohl, 1997). The genes dpsC and -D are rare, and equivalent enzymes have only been described in this and other type II PKS clusters that utilize nonacetate starters (Bibb et al., 1994; Piel et al., 2000; Raty et al., 2002). Their role in starter unit selection is not, however, entirely clear, as deleting dpsC but not dpsD shifted starter unit selection from propionate to predominantly acetate (Rajgarhia and Strohl, 1997), suggesting that dpsC and not dpsD contributes to, but does not dictate, starter unit selection.
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Present address: Department of Microbiology, Biological Process Technology Institute, University of Minnesota, St. Paul, MN 55108, U.S.A. Tel. (1-612) 625-1901