ArticleApplied and environmental microbiology2003
Involvement of two cytosolic enzymes and a novel intermediate, 5'-oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in aflatoxin biosynthesis.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 26 citations in OpenAlex.
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- Lifestyle Transitions in Fusarioid Fungi are Frequent and Lack Clear Genomic Signatures.Molecular biology and evolution · 2022Article
- Characteristics, Occurrence, Detection and Detoxification of Aflatoxins in Foods and Feeds.Foods (Basel, Switzerland) · 2020Review
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- Complete biosynthetic pathways of ascofuranone and ascochlorin inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Biosynthesis of oxygen and nitrogen-containing heterocycles in polyketides.Beilstein journal of organic chemistry · 2016Review
- Current understanding on aflatoxin biosynthesis and future perspective in reducing aflatoxin contamination.Toxins · 2012Review
- Genetics of Polyketide Metabolism in Aspergillus nidulans.Metabolites · 2012Article
- Functional expression and subcellular localization of the aflatoxin pathway enzyme Ver-1 fused to enhanced green fluorescent protein.Applied and environmental microbiology · 2008Article
- Function of the cypX and moxY genes in aflatoxin biosynthesis in Aspergillus parasiticus.Applied and environmental microbiology · 2005Article
- Aspergillus parasiticus cyclase catalyzes two dehydration steps in aflatoxin biosynthesis.Applied and environmental microbiology · 2005Article
- Clustered pathway genes in aflatoxin biosynthesis.Applied and environmental microbiology · 2004Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During aflatoxin biosynthesis, 5'-hydroxyaverantin (HAVN) is converted to averufin (AVR). Although we had previously suggested that this occurs in one enzymatic step, we demonstrate here that this conversion is composed of two enzymatic steps by showing that the two enzyme activities in the cytosol fraction of Aspergillus parasiticus were clearly separated by Mono Q column chromatography. An enzyme, HAVN dehydrogenase, catalyzes the first reaction from HAVN to a novel intermediate, another new enzyme catalyzes the next reaction from the intermediate to AVR, and the intermediate is a novel substance, 5'-oxoaverantin (OAVN), which was determined by physicochemical methods. We also purified both of the enzymes, HAVN dehydrogenase and OAVN cyclase, from the cytosol fraction of A. parasiticus by using ammonium sulfate fractionation and successive chromatographic steps. The HAVN dehydrogenase is a homodimer composed of 28-kDa subunits, and it requires NAD, but not NADP, as a cofactor for its activity. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis of tryptic peptides of the purified HAVN dehydrogenase revealed that this enzyme coincides with a protein deduced from the adhA gene in the aflatoxin gene cluster of A. parasiticus. Also, the OAVN cyclase enzyme is a homodimer composed of 79-kDa subunits which does not require any cofactor for its activity. Further characterizations of both enzymes were performed.
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