Microginin FR1, a linear peptide from a water bloom of Microcystis species

A so far unknown structural variant, called microginin FR1, of cyanobacterial peptides of the microginin type was isolated from a water bloom of a German lake. The bloom consisted almost exclusively of Microcystis sp. cells. The structure of microginin FR1 was identified by amino acid analysis, dete...

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Bibliographic Details
Published in:FEMS microbiology letters 1997-08, Vol.153 (2), p.475-478
Main Authors: Neumann, U, Forchert, A, Flury, T, Weckesser, J
Format: Article
Language:English
Subjects:
Alanine
Amino acids
Angiotensin
Angiotensin‐converting enzyme inhibition
animal health
human health and safety
Leucine
Mass spectrometry
Mass spectroscopy
medicine
Microbiology
Microcystis
Microcystis sp
Microginin FR1
NMR
Nuclear magnetic resonance
Peptide
Peptides
Peptidyl-dipeptidase A
Tyrosine
veterinary medicine
Water analysis
Water bloom
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Summary:A so far unknown structural variant, called microginin FR1, of cyanobacterial peptides of the microginin type was isolated from a water bloom of a German lake. The bloom consisted almost exclusively of Microcystis sp. cells. The structure of microginin FR1 was identified by amino acid analysis, determination of the relative molecular mass by electrospray mass spectrometry, and by NMR to be a linear pentapeptide with a relative molecular mass of 727 which contains a beta-amino-alpha-hydroxy-decanoic acid (Ahda), alanine, N-methyl-leucine, and two tyrosine units (Ahda-Ala-N-Me-Leu-Tyr-Tyr). Microginin FR1 had angiotensin-converting enzyme inhibitory activity with half-maximal inhibition at 6 x 10(-5) M microginin FR1.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1997.tb12612.x