ArticleScientific reports2015
A novel cysteine desulfurase influencing organosulfur compounds in Lentinula edodes.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 32 citations in OpenAlex.
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- Regulation of Mitochondrial Respiration by Hydrogen Sulfide.Antioxidants (Basel, Switzerland) · 2023Review
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- A global phylogenomic analysis of the shiitake genusProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Effects of Drying Process on the Volatile and Non-Volatile Flavor Compounds ofFoods (Basel, Switzerland) · 2021Article
- Effects of enzymatic reaction on the generation of key aroma volatiles in shiitake mushroom at different cultivation substrates.Food science & nutrition · 2021Article
- Interplay Among Hydrogen Sulfide, Nitric Oxide, Reactive Oxygen Species, and Mitochondrial DNA Oxidative Damage.Frontiers in plant science · 2021Review
- Effects of GGT and C-S Lyase on the Generation of Endogenous Formaldehyde inMolecules (Basel, Switzerland) · 2019Article
- Identification of a Heat-Inducible Element of Cysteine Desulfurase Gene Promoter inMolecules (Basel, Switzerland) · 2019Article
- The role of metals in mammalian olfaction of low molecular weight organosulfur compounds.Natural product reports · 2017Review
- Genome Sequence of the Edible Cultivated Mushroom Lentinula edodes (Shiitake) Reveals Insights into Lignocellulose Degradation.PloS one · 2016Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Organosulfur compounds are the basis for the unique aroma of Lentinula edodes, and cysteine sulfoxide lyase (C-S lyase) is the key enzyme in this trait. The enzyme from Alliium sativum has been crystallized and well-characterized; however, there have been no reports of the characterization of fungi C-S lyase at the molecular level. We identified a L. edodes C-S lyase (Lecsl), cloned a gene of Csl encoded Lecsl and then combined modeling, simulations, and experiments to understand the molecular basis of the function of Lecsl. Our analysis revealed Lecsl to be a novel cysteine desulfurase and not a type of cysteine sulfoxide lyase. The pyridoxal-5-phosphate (PLP) molecule bonded tightly to Lecsl to form a Lecsl-PLP complex. Moreover, the Lecsl had one active center that served to bind two kinds of substrates, S-methyl-L-cysteine sulfoxide and L-cysteine, and had both cysteine sulfoxide lyase and cysteine desulfurase activity. We found that the amino acid residue Asn393 was essential for the catalytic activity of Lecsl and that the gene Csl encoded a novel cysteine desulfurase to influence organosulfur compounds in L. edodes. Our results provide a new insight into understanding the formation of the unique aroma of L. edodes.
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