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

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. Wit...