F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales.
Two classes of F(420)-dependent reductases (FDR-A and FDR-B) that can reduce aflatoxins and thereby degrade them have previously been isolated from Mycobacterium smegmatis. One class, the FDR-A enzymes, has up to 100 times more activity than the other. F(420) is a cofactor with a low reduction poten...
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Public Library of Science (PLoS)
2012-01-01
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Online Access: | http://europepmc.org/articles/PMC3288000?pdf=render |
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author | Gauri V Lapalikar Matthew C Taylor Andrew C Warden Colin Scott Robyn J Russell John G Oakeshott |
author_facet | Gauri V Lapalikar Matthew C Taylor Andrew C Warden Colin Scott Robyn J Russell John G Oakeshott |
author_sort | Gauri V Lapalikar |
collection | DOAJ |
description | Two classes of F(420)-dependent reductases (FDR-A and FDR-B) that can reduce aflatoxins and thereby degrade them have previously been isolated from Mycobacterium smegmatis. One class, the FDR-A enzymes, has up to 100 times more activity than the other. F(420) is a cofactor with a low reduction potential that is largely confined to the Actinomycetales and some Archaea and Proteobacteria. We have heterologously expressed ten FDR-A enzymes from diverse Actinomycetales, finding that nine can also use F(420)H(2) to reduce aflatoxin. Thus FDR-As may be responsible for the previously observed degradation of aflatoxin in other Actinomycetales. The one FDR-A enzyme that we found not to reduce aflatoxin belonged to a distinct clade (herein denoted FDR-AA), and our subsequent expression and analysis of seven other FDR-AAs from M. smegmatis found that none could reduce aflatoxin. Certain FDR-A and FDR-B enzymes that could reduce aflatoxin also showed activity with coumarin and three furanocoumarins (angelicin, 8-methoxysporalen and imperatorin), but none of the FDR-AAs tested showed any of these activities. The shared feature of the compounds that were substrates was an α,β-unsaturated lactone moiety. This moiety occurs in a wide variety of otherwise recalcitrant xenobiotics and antibiotics, so the FDR-As and FDR-Bs may have evolved to harness the reducing power of F(420) to metabolise such compounds. Mass spectrometry on the products of the FDR-catalyzed reduction of coumarin and the other furanocoumarins shows their spontaneous hydrolysis to multiple products. |
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spelling | doaj.art-06358edfb8334964a2b5d9f0fbc2ed112022-12-21T23:52:50ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0172e3011410.1371/journal.pone.0030114F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales.Gauri V LapalikarMatthew C TaylorAndrew C WardenColin ScottRobyn J RussellJohn G OakeshottTwo classes of F(420)-dependent reductases (FDR-A and FDR-B) that can reduce aflatoxins and thereby degrade them have previously been isolated from Mycobacterium smegmatis. One class, the FDR-A enzymes, has up to 100 times more activity than the other. F(420) is a cofactor with a low reduction potential that is largely confined to the Actinomycetales and some Archaea and Proteobacteria. We have heterologously expressed ten FDR-A enzymes from diverse Actinomycetales, finding that nine can also use F(420)H(2) to reduce aflatoxin. Thus FDR-As may be responsible for the previously observed degradation of aflatoxin in other Actinomycetales. The one FDR-A enzyme that we found not to reduce aflatoxin belonged to a distinct clade (herein denoted FDR-AA), and our subsequent expression and analysis of seven other FDR-AAs from M. smegmatis found that none could reduce aflatoxin. Certain FDR-A and FDR-B enzymes that could reduce aflatoxin also showed activity with coumarin and three furanocoumarins (angelicin, 8-methoxysporalen and imperatorin), but none of the FDR-AAs tested showed any of these activities. The shared feature of the compounds that were substrates was an α,β-unsaturated lactone moiety. This moiety occurs in a wide variety of otherwise recalcitrant xenobiotics and antibiotics, so the FDR-As and FDR-Bs may have evolved to harness the reducing power of F(420) to metabolise such compounds. Mass spectrometry on the products of the FDR-catalyzed reduction of coumarin and the other furanocoumarins shows their spontaneous hydrolysis to multiple products.http://europepmc.org/articles/PMC3288000?pdf=render |
spellingShingle | Gauri V Lapalikar Matthew C Taylor Andrew C Warden Colin Scott Robyn J Russell John G Oakeshott F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. PLoS ONE |
title | F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. |
title_full | F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. |
title_fullStr | F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. |
title_full_unstemmed | F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. |
title_short | F420H2-dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales. |
title_sort | f420h2 dependent degradation of aflatoxin and other furanocoumarins is widespread throughout the actinomycetales |
url | http://europepmc.org/articles/PMC3288000?pdf=render |
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