Two novel diketopiperazines isolated from the fungus Tolypocladium sp.

Chu, Min; Mierzwa, Ronald; Truumees, Imbi; Gentile, Frank; Patel, Mahesh; Gullo, Vincent P.; Chan, Tze‐Ming; Puar, Mohindar S.

doi:10.1016/s0040-4039(00)60393-3

Cited by 48 publications

(49 citation statements)

References 3 publications

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“…The signal of H-19 of the dimethylallyl moiety at 4.45 p.p.m. indicated that the prenyl moiety was attached to a hetero atom (Chu et al, 1993;Yin et al, 2007), rather than a carbon atom. In the case of a C-C connection, the signal of H-19 would be found in the range of 3.4-3.8 p.p.m.…”

Section: Enzymic Activity Of Sird and Identification Of The Enzymic mentioning

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: Enzymic Activity Of Sird and Identification Of The Enzymic mentioning

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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“…), as well as compounds 52 and 53, which had been originally isolated from a fermentation of the fungus Tolypocladium sp. [60]. The absolute configurations of 52 and 53 were determined by chemical transformations [61].…”

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confidence: 99%

Diketopiperazines from Marine Organisms

Huang

Zhou

Tian

et al. 2010

Chemistry & Biodiversity

144

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Diketopiperazines (DKPs), which are cyclic dipeptides, have been detected in a variety of natural resources. Recently, the interest in these compounds increased significantly because of their remarkable bioactivity. This review deals with the chemical structures, biosynthetic pathways, and biological activities of DKPs from marine microorganisms, sponges, sea stars, tunicates (ascidians), and red algae. The literature has been covered up to December 2008, and a total 124 DKPs from 104 publications have been discussed and reviewed. Some of these compounds have been found to possess various bioactivities including cytotoxicity, and antibacterial, antifungal, antifouling, plant-growth regulatory, and other activities.

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“…[1,2] Their derivatives have been used widely in the inhibition of the cell growth cycles of mammals, [3] the inhibition of glutathione-S-transferase, [4] the inhibition of the activated factor of thrombocytes, [5] and as inhibitors of various enzymes including topoisomerases and collagenase-1. [6,7] The effect of introduction of a sulfur or selenium atom into these molecules has not been tested.…”

Section: Introductionmentioning

confidence: 99%

Selenation/Thionation of α‐Amino Acids: Formation and X‐ray Structures of Diselenopiperazine and Dithiopiperazine and Related Compounds

et al. 2011

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N‐Phenylglycine reacts with an equivalent of 2,4‐bis(phenyl)‐1,3‐diselenadiphosphetane 2,4‐diselenide (Woollins' reagent, WR) to generate as the major product 1,4‐diphenylpiperazine‐2,5‐diselenone and as the minor product 1,4‐diphenyl‐5‐selenoxopiperazin‐2‐one. Whereas, reacting N‐phenylglycine with an equivalent of 2,4‐bis(4‐methoxyphenyl)‐1,3‐dithia‐2,4‐diphosphetane 2,4‐disulfide (Lawesson's reagent, LR) affords 1,4‐diphenylpiperazine‐2,5‐dithione and N‐phenyl‐2‐(phenylamino)ethanethioamide. 2‐Phenylglycine treated with an equivalent of Woollins' reagent under identical reaction conditions leads to only the formation of 2,5‐diphenylpyrazine. Six X‐ray structures are reported. DFT‐B3LYP calculations suggest that the planar conformation is around 2 kcal/mol less stable than the puckered conformation for the bis‐seleno derivative.

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Two novel diketopiperazines isolated from the fungus Tolypocladium sp.

Cited by 48 publications

References 3 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

Diketopiperazines from Marine Organisms

Selenation/Thionation of α‐Amino Acids: Formation and X‐ray Structures of Diselenopiperazine and Dithiopiperazine and Related Compounds

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