The metabolism of the non-proteinogenic amino acid β-N-methylamino-L-alanine (BMAA) in the cyanobacterium Synechocystis PCC6803. (1st June 2016)

• Record Type: Journal Article
• Authors: Downing, Simoné; Downing, Timothy Grant
• Is Part Of: Toxicon. Volume 115(2016)
• Page Start: 41
• Page End: 48
• Publication Date: 2016-06-01
• Subjects: β-N-methylamino-L-alanine -- BMAA -- Cyanobacteria -- Metabolism -- Biosynthesis -- Synechocystis PCC6803; Toxins -- Periodicals; Venom -- Periodicals; 615.9
• DOI: 10.1016/j.toxicon.2016.03.005
• Languages: English
• ISSNs: 0041-0101

Abstract

Abstract: The neurotoxic amino acid β- N -methylamino-L-alanine (BMAA) is produced by cyanobacteria under nitrogen starvation conditions and its metabolism is closely associated with cellular nitrogen control. Very little is known regarding the metabolism or biosynthesis of this amino acid in the producing organisms and current knowledge is limited to the spontaneous formation of carbamate adducts in the presence of aqueous carbon dioxide, the rapid removal of free cellular BMAA upon the addition of ammonia to nitrogen-starved cyanobacterial cultures, and the link between cellular nitrogen status and BMAA synthesis. Data presented here show that exogenous BMAA is readily metabolised by cyanobacteria during which, the primary amino group is rapidly transferred to other cellular amino acids. Furthermore, data suggest that BMAA is metabolised in cyanobacteria via a reversible transamination reaction. This study presents novel data on BMAA metabolism in cyanobacteria and provides the first proposed biosynthetic precursor to BMAA biosynthesis in cyanobacteria. Highlights: In Synechocystis PCC6803 BMAA metabolism involves transamination reactions with the primary amino group. In cyanobacteria, β- N -methylamino-L-alanine metabolism does not involve deamination of primary amino group. Transamination of BMAA in Synechocystis PCC6803 appears to be catalysed by glutamine oxoglutarate aminotransferase.