Chromane derivatives of small aromatic molecules: Chemoenzymatic synthesis and growth inhibitory activity on human tumor cell line LoVo WT

Macone, Alberto; Lendaro, Eugenio; Comandini, Alessandra; Rovardi, Irene; Matarese, Rosa Marina; Carraturo, Antonio; Bonamore, Alessandra

doi:10.1016/j.bmc.2009.06.061

Cited by 12 publications

(8 citation statements)

References 28 publications

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“…CdpNPT and AnaPT also catalyse both C-and N-prenylation . The ability of prenyltransferases to catalyse Cprenylation is of special importance, as it can be used in the production of prenylated derivatives (Li, 2009a;Macone et al, 2009).…”

Section: Substratementioning

confidence: 99%

A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL

Kremer

2010

Microbiology

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A putative prenyltransferase gene sirD has been identified in the gene cluster encoding the biosynthesis of the phytotoxin sirodesmin PL in Leptosphaeria maculans. The gene product was found to comprise 449 aa, with a molecular mass of 51 kDa. In this study, the coding region of sirD was amplified by PCR from cDNA, cloned into pQE70, and overexpressed in Escherichia coli. The overproduced protein was purified to apparent homogeneity, and characterized biochemically. The dimeric recombinant SirD was found to catalyse the O-prenylation of L-Tyr in the presence of dimethylallyl diphosphate; this was demonstrated unequivocally by isolation and structural elucidation of the enzymic product. Therefore, SirD catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL. K m values for L-Tyr and dimethylallyl diphosphate were determined as 0.13 and 0.17 mM, respectively. Interestingly, SirD was found to share significant sequence similarity with indole prenyltransferases, which catalyse prenyl transfer reactions onto different positions of indole rings. In contrast to indole prenyltransferases, which accept indole derivatives, but not Tyr or structures derived thereof, as substrates, SirD also prenylated L-Trp, resulting in the formation of 7-dimethylallyltryptophan. A K m value of 0.23 mM was determined for L-Trp. Turnover numbers of 1.0 and 0.06 S "1 were calculated for L-Tyr and L-Trp, respectively.

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Section: Substratementioning

confidence: 99%

A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL

Kremer

2010

Microbiology

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“…Moreover, the existence of a ring 3′-OH makes the catalytic mechanism different from that of ring formation catalyzed by Fe 3+ [2] or chalcone isomerase [23]–[32]. We hypothesized that an oxidative cyclization catalyzed by XimD and XimE are plausible.…”

Section: Discussionmentioning

confidence: 98%

“…Among those that are produced, benzopyran and its derivatives generally have low cellular toxicity and good membrane permeability [2]. One example is xiamenmycin ( 1 ), which in 2000 was reported to be an inhibitor of ICAM-1/LFA-1 interaction with a possible anti-inflammatory function [3].…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Xiamenmycin Biosynthesis Gene Cluster in Streptomyces xiamenensis 318

Yang

Zhang

et al. 2014

PLoS ONE

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Xiamenmycin (1) is a prenylated benzopyran derivative with anti-fibrotic activity. To investigate the genetic basis of xiamenmycin biosynthesis, we performed genome mining in the xiamenmycin-producing Streptomyces xiamenensis wild-type strain 318 to identify a candidate gene cluster. The complete gene cluster, consisting of five genes, was confirmed by a series of gene inactivations and heterologous expression. Based on bioinformatics analyses of each gene and feeding experiments, we found that the structure of an intermediate xiamenmycin B (3) accumulated in a ximA inactivation mutant, allowing us to propose a biosynthetic pathway. All five of the genes in the pathway were genetically and biochemically characterized. XimA was biochemically characterized as an ATP-dependent amide synthetase, catalyzing an amide bond formation in the presence of ATP as the final step in Xiamenmycin biosynthesis. The K m value of XimA was determined to be 474.38 µM for the substrate xiamenmycin B. These studies provide opportunities to use genetic and chemo-enzymatic methods to create new benzopyran derivatives as potential therapeutic agents.

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“…Reyes-Zurita et al found that maslinic acid induces apoptosis in HT29 colon cancer cells via the mitochondrial apoptotic pathway [69]. Furthermore, NPs with other structures, such as polyacetylenes and polyenes [72], chromane derivatives [73], grifolin [74], g-oryzanol [75], yuanhuacine [76], chartreusin [77] and statins [78], have been explored for the purpose of drug discovery for CRC ( Table 5). In addition, NPs derived from organisms in marine environments have recently been investigated.…”

Section: Other Nps For Anti-cancer Drug Discoverymentioning

confidence: 98%

“…Honokiol [65], magnolol [66], podophyllotoxin, silibinin, hydnocarpin Substances other than polyphenols Alkaloids Antofine [67,68], avenanthramide, neo-clerodane diterpenoid alkaloids, taspine Terpenes Maslinic acid [69], talaporfin, novel triterpenoids, ent-clerodane diterpenoids, curcuphenol, picrotoxin, solaniol, triptolide, carnosic acid, koetjapic acid, andrographolide, plaunotol, geranylgeraniol Sapogenin Yerba mate tea and mate saponins [70], Paris saponin VII [71] Other substances Polyacetylenes and polyenes [72], chromane derivatives [73], grifolin [74], g-oryzanol [75], yuanhuacine [76], chartreusin [77], simvastatin and lovastatin [78], TPU942 and its derivatives [79], PTZ0025, phytic acid, b-sitosterol, diallyl sulfide, brefeldin A, parthenolide, norcantharidin, protopanaxadiol, melanoidin, evodiamine, 1'-acetoxychavicol acetate, panaxadiol, renieramycin, pyrazolone derivatives, b-asarone, phthalide, turmerone…”

Section: Polyphenolsmentioning

confidence: 99%

The use of natural products in colorectal cancer drug discovery

Miura

Satoh

Kinouchi

et al. 2015

Expert Opinion on Drug Discovery

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Chromane derivatives of small aromatic molecules: Chemoenzymatic synthesis and growth inhibitory activity on human tumor cell line LoVo WT

Cited by 12 publications

References 28 publications

A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL

A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL

Characterization of the Xiamenmycin Biosynthesis Gene Cluster in Streptomyces xiamenensis 318

The use of natural products in colorectal cancer drug discovery

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