Isolation and structure determination of a new analog of polycavernosides from marine Okeania sp. cyanobacterium

• Kairi Umeda,
• Naoaki Kurisawa,
• Ghulam Jeelani,
• Tomoyoshi Nozaki,
• Kiyotake Suenaga and
• Arihiro Iwasaki

Beilstein J. Org. Chem. 2024, 20, 645–652, doi:10.3762/bjoc.20.57

• polycavernosides. Keywords: macrolide glycoside; marine cyanobacterium; marine natural products; polycavernosides; terminal alkyne; Introduction In 1991, an outbreak of food poisoning caused by a species of red algae known as ‘Polycavernosa tsudai’ occurred in Guam, which resulted in killing of three people. Two

• the sample The marine cyanobacterium producing polycavernoside E (1) was collected in March 2022 at the coast in Akuna beach, Yonashiromiyagi, Uruma city, Okinawa, Japan. It was classified into Okeania sp. based on the phylogenetic analysis as described in the previous paper (accession no. LC771053

First total synthesis of hoshinoamide A

• Haipin Zhou,
• Zihan Rui,
• Yiming Yang,
• Shengtao Xu,
• Yutian Shao and
• Long Liu

Beilstein J. Org. Chem. 2021, 17, 2924–2931, doi:10.3762/bjoc.17.201

• 210009, China Taizhou Medical Hi-Tech Development Public Services Platform, Taizhou 225300, China 10.3762/bjoc.17.201 Abstract Hoshinoamides A, B and C, linear lipopeptides, were isolated from the marine cyanobacterium Caldora penicillata, with potent antiplasmodial activity against chloroquine

• , hoshinoamides A, B [11] and C [12], from a microbial metabolite of marine cyanobacterium Caldora penicillata (Figure 1). Hoshinoamides A and B showed potent activities against chloroquine-sensitive Plasmodium falciparum 3D7 with IC50 values of 0.52 and 1.0 μM, respectively. Hoshinoamide C inhibited the growth

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• necessary to finally yield anatoxin-a and homoanatoxin-a [38]. NRPS and PKS pathways in marine cyanobacteria Barbamide Several NRPS/PKS assembly lines were identified and partially characterized for the marine cyanobacterium Lyngbya majuscula [39]. These filamentous tropical cyanobacteria are important

• second biosynthetic pathway identified in a strain of the tropical marine cyanobacterium Lyngbya majuscula was assigned to jamaicamides 8. Jamaicamides are neurotoxins and show sodium-channel-blocking activity. The lipopeptide is highly functionalized and contains a bromo-alkynyl, a chlorovinylidene

• marine cyanobacterium [69]. A single LanM-type enzyme, ProcM, was found to cooperate with 29 different precursor peptides in vitro and in vivo. The enzyme thus showed a remarkable catalytic promiscuity. The precursor peptides were encoded either cis or trans to the ProcM enzyme, and the resulting family