scholarly journals UV Protective Compounds Mycosporine-like Amino Acids (MAAs) and Bloom Forming Mechanism in Microcystis aeruginosa

2003 ◽  
Vol 15 (4) ◽  
pp. 359-363 ◽  
Author(s):  
LIU Zhengwen ◽  
◽  
ZHONG Ping ◽  
HAN Boping
1959 ◽  
Vol 37 (1) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.


2020 ◽  
Author(s):  
Sandip Radhakisan Ugale ◽  
Somnath S Gholap

Abstract: A formal total synthesis of Balgacyclamide A as an antimalarial cynobactin of Microcystis aeruginosa (EAWAG 251) has been described. The synthesis of titled cyclamide was accomplished by the solution phase fragment synthesis using protection, deprotection and macrocylization process. Four common amino acids such as d-alanine, l-threonine, l-valine and d-allo-isoleucine, has been used for the construction of Balgacyclamide A. Including, the oxazoline and thiazole are the core structures was successfully achieved by using Burgess reagent and Hantzsch methods. The overall yield of the synthesized balgacyclamide A was found to be 2.03%, also structure was confirmed by1H-NMR, 13C-NMR and HRMS spectral data.


2009 ◽  
Vol 161 (2-3) ◽  
pp. 730-736 ◽  
Author(s):  
Ruihua Dai ◽  
Huijuan Liu ◽  
Jiuhui Qu ◽  
Xu Zhao ◽  
Yining Hou

2020 ◽  
Author(s):  
Meng Chen ◽  
Chun-Yang Xu ◽  
Xu Wang ◽  
Chong-Yang Ren ◽  
Jiao Ding ◽  
...  

Abstract Background : Cyanobacteria are of special concern because they proliferate in eutrophic water bodies worldwide and affect water quality. As an ancient photosynthetic microorganism, cyanobacteria can survive in ecologically diverse habitats because of their capacity to rapidly respond to environmental changes through a web of complex signaling networks, including using second messengers to regulate physiology or metabolism. A ubiquitous second messenger, bis-(3′,5′)-cyclic-dimeric-guanosine monophosphate (c-di-GMP), has been found to regulate essential behaviors in a few cyanobacteria but not Microcystis, which are the most dominant species in cyanobacterial blooms. In this study, comparative genomics analysis was performed to explore the genomic basis of c-di-GMP signaling in Microcystis aeruginosa . Results: Proteins involved in c-di-GMP metabolism and regulation, such as diguanylate cyclases, phosphodiesterases, and PilZ-containing proteins, were encoded in M. aeruginosa genomes. However, the number of identified protein domains involved in c-di-GMP signaling was not proportional to the size of M. aeruginosa genomes (4.97 Mb in average). Pan-genome analysis showed that genes involved in c-di-GMP metabolism and regulation are conservative in M. aeruginosa strains. Phylogenetic analysis showed good congruence between the two types of phylogenetic trees based on 31 highly conserved protein-coding genes and sensor domain-coding genes. Propensity for gene loss analysis revealed that most of genes involved in c-di-GMP signaling are stable in M. aeruginosa strains. Moreover, bioinformatics and structure analysis of c-di-GMP signal-related GGDEF and EAL domains revealed that they all possess essential conserved amino acid residues that bind the substrate. In addition, it was also found that all selected M. aeruginosa genomes encode PilZ domain containing proteins. Conclusions: Comparative genomics analysis of c-di-GMP metabolism and regulation in M. aeruginosa strains helped elucidating the genetic basis of c-di-GMP signaling pathways in M. aeruginosa. Knowledge of c-di-GMP metabolism and relevant signal regulatory processes in cyanobacteria can enhance our understanding of their adaptability to various environments and bloom-forming mechanism.


1959 ◽  
Vol 37 (3) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.


RSC Advances ◽  
2016 ◽  
Vol 6 (65) ◽  
pp. 60869-60876 ◽  
Author(s):  
Cheng Liu ◽  
Siyuan He ◽  
Zhehao Sun ◽  
Jie Wang ◽  
Wei Chen

Main categories of typical proteins and amino acids derived fromM. aeruginosawere identified and their removal by MIEX® was discussed.


1970 ◽  
Vol 48 (4) ◽  
pp. 508-510 ◽  
Author(s):  
J. Rama Murthy ◽  
J. B. Capindale

The endotoxin from the blue–green alga Microcystis aeruginosa NRC-1 has been isolated as its ammonium salt by a new procedure involving solvent extraction and elution from DEAE-Sephadex A-25. The intraperitoneal LD100 of this toxin preparation for mice was 0.1 mg/kg body weight. The product is a white solid which appears to be chromatographically and electrophoretically homogeneous. This toxin produces similar symptoms in mice to those described originally for the toxic material from the same algal strain. Analysis of the toxin hydrolysate indicates a more complex structure since seven more amino acids have been found, including tyrosine, proline, and arginine, in addition to the seven reported before.


1989 ◽  
Vol 151 (5) ◽  
pp. 411-415 ◽  
Author(s):  
I. M. Birk ◽  
R. Dierstein ◽  
I. Kaiser ◽  
U. Matern ◽  
W. A. König ◽  
...  

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