Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2
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...
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| Published in | Archives of microbiology Vol. 202; no. 6; pp. 1419 - 1424 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
01.08.2020
Springer Nature B.V |
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| Abstract | 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. |
|---|---|
| AbstractList | 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. 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. 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.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. |
| Author | Fan, Aili Yang, Keyan Li, Shu-Ming Liu, Xiaoqing |
| Author_xml | – sequence: 1 givenname: Keyan surname: Yang fullname: Yang, Keyan organization: College of Life Science, Capital Normal University – sequence: 2 givenname: Shu-Ming surname: Li fullname: Li, Shu-Ming organization: Institut für Pharmazeutische Biologie Und Biotechnologie, Philipps-Universität Marburg – sequence: 3 givenname: Xiaoqing surname: Liu fullname: Liu, Xiaoqing email: liuxq@cnu.edu.cn organization: College of Life Science, Capital Normal University – sequence: 4 givenname: Aili orcidid: 0000-0003-4738-0517 surname: Fan fullname: Fan, Aili email: fanal@mail.buct.edu.cn organization: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32185409$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1074/jbc.M111.317982 10.1016/j.phytochem.2009.08.023 10.1016/B978-0-12-394291-3.00005-8 10.1021/ja1049302 10.1007/s00253-015-6811-y 10.1007/s00253-012-4130-0 10.1073/pnas.90.14.6791 10.1016/j.febslet.2007.05.031 10.1021/cb500791f 10.1007/s004380050950 10.1007/s00253-009-2128-z 10.15227/orgsyn.066.0211 10.1021/acs.orglett.7b02926 10.1016/S0968-0896(03)00308-0 10.1099/mic.0.27962-0 10.1016/j.cbpa.2009.02.020 10.1038/ja.2010.128 10.1099/mic.0.069542-0 10.1021/ol503399b |
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| Keywords | Substrate promiscuity Prenyltransferase Enzyme catalysis DMATS NotF BrePT |
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| Snippet | NotF from
Aspergillus
sp. MF297-2 and BrePT from
Aspergillus versicolor
catalyze a reverse C2-prenylation of brevianamide F in the biosynthetic pathway of... NotF from Aspergillus sp. MF297-2 and BrePT from Aspergillus versicolor catalyze a reverse C2-prenylation of brevianamide F in the biosynthetic pathway of... |
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| SubjectTerms | 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 |
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| Title | Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2 |
| URI | https://link.springer.com/article/10.1007/s00203-020-01854-7 https://www.ncbi.nlm.nih.gov/pubmed/32185409 https://www.proquest.com/docview/2422918347 https://www.proquest.com/docview/2378898869 https://www.proquest.com/docview/2551980635 |
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