scholarly journals Indole Derivatives Produced by the Metagenome Genes of the Escherichia coli-Harboring Marine Sponge Discodermia calyx

Molecules ◽  
2017 ◽  
Vol 22 (5) ◽  
pp. 681 ◽  
Author(s):  
Feng-Lou Liu ◽  
Xiao-Long Yang
Keyword(s):  
Escherichia Coli ◽  
Marine Sponge ◽  
Indole Derivatives ◽  
Discodermia Calyx

Two new indole derivatives from a marine sponge Ircinia sp. collected at Iriomote Island

2015 ◽  
Vol 69 (3) ◽  
pp. 416-420 ◽  
Author(s):  
Delfly B. Abdjul ◽  
Hiroyuki Yamazaki ◽  
Kazuyo Ukai ◽  
Michio Namikoshi
Keyword(s):  
Marine Sponge ◽  
Indole Derivatives ◽  
Iriomote Island

Allos-hemicalyculin A, a photochemically converted calyculin from the marine sponge Discodermia calyx

2013 ◽  
Vol 54 (1) ◽  
pp. 114-116 ◽  
Author(s):  
Miki Kimura ◽  
Toshiyuki Wakimoto ◽  
Ikuro Abe
Keyword(s):  
Marine Sponge ◽  
Discodermia Calyx

Calyculins E, F, G, and H, additional inhibitors of protein phosphatases 1 and 2a, from the marine sponge discodermia calyx

Tetrahedron ◽  
1991 ◽  
Vol 47 (18-19) ◽  
pp. 2999-3006 ◽  
Author(s):  
Shigeki Matsunaga ◽  
Hirota Fujiki ◽  
Daisuke Sakata ◽  
Nobuhiro Fusetani
Keyword(s):  
Marine Sponge ◽  
Protein Phosphatases ◽  
Discodermia Calyx

Isolation of dephosphonocalyculin a from the marine sponge, Discodermia calyx

1997 ◽  
Vol 38 (21) ◽  
pp. 3763-3764 ◽  
Author(s):  
Shigeki Matsunaga ◽  
Toshiyuki Wakimoto ◽  
Nobuhiro Fusetani ◽  
Masami Suganuma
Keyword(s):  
Marine Sponge ◽  
Discodermia Calyx

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

Microbiology ◽  
2010 ◽  
Vol 156 (1) ◽  
pp. 278-286 ◽  
Author(s):  
Anika Kremer ◽  
Shu-Ming Li
Keyword(s):  
Escherichia Coli ◽  
Sequence Similarity ◽  
Leptosphaeria Maculans ◽  
Transfer Reactions ◽  
Indole Derivatives ◽  
Coding Region ◽  
Significant Sequence Similarity ◽  
Dimethylallyl Diphosphate ◽  
Apparent Homogeneity ◽  
Specific Step

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.

Indole Derivatives from a Marine Sponge-Derived Yeast as DPPH Radical Scavengers

2009 ◽  
Vol 72 (11) ◽  
pp. 2069-2071 ◽  
Author(s):  
Yasumasa Sugiyama ◽  
Yuki Ito ◽  
Motofumi Suzuki ◽  
Akira Hirota
Keyword(s):  
Marine Sponge ◽  
Indole Derivatives ◽  
Dpph Radical ◽  
Radical Scavengers
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