Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2

• Published in: Archives of microbiology Vol. 202; no. 6; pp. 1419 - 1424
• Main Authors: Yang, Keyan, Li, Shu-Ming, Liu, Xiaoqing, Fan, Aili
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.08.2020; Springer Nature B.V
• Subjects: Amino acids; Aspergillus; Aspergillus - genetics; Aspergillus - metabolism; Aspergillus versicolor; biochemical pathways; Biochemistry; Biomedical and Life Sciences; Biotechnology; Cell Biology; dimethylallyltranstransferase; Dimethylallyltranstransferase - chemistry; Dimethylallyltranstransferase - genetics; Dimethylallyltranstransferase - metabolism; Ecology; Indole Alkaloids - metabolism; Life Sciences; Microbial Ecology; Microbiology; Original Paper; Prenylation; Prenyltransferases; Substrate Specificity; Substrates; Substrate promiscuity; Prenyltransferase; Enzyme catalysis; DMATS; NotF; BrePT
• ISSN: 0302-8933; 1432-072X; 1432-072X
• DOI: 10.1007/s00203-020-01854-7

NotF from Aspergillus sp. MF297-2 and BrePT from Aspergillus versicolor catalyze a reverse C2-prenylation of brevianamide F in the biosynthetic pathway of brevianamides and notoamides. NotF was reported to use only brevianamide F as substrate while BrePT demonstrated broad substrate promiscuity. With high identity at amino acid level, it is interesting to reinvestigate the catalytic activities of these two prenyltransferases in vitro toward 14 cyclodipeptides. Product identification of the in vitro assays by MS proved that NotF and BrePT share similar catalytic ability and substrate promiscuity.