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Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to constitute 1% of all described fungal species.
Saccharomyces cerevisiae is a species of yeast. The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular and cell biology, much like Escherichia coli as the model bacterium. It is the microorganism behind the most common type of fermentation. S. cerevisiae cells are round to ovoid, 5–10 μm in diameter. It reproduces by budding.
Ergosterol (ergosta-5,7,22-trien-3β-ol) is a sterol found in cell membranes of fungi and protozoa, serving many of the same functions that cholesterol serves in animal cells. Because many fungi and protozoa cannot survive without ergosterol, the enzymes that synthesize it have become important targets for drug discovery. In human nutrition, ergosterol is a provitamin form of vitamin D2; exposure to ultraviolet (UV) light causes a chemical reaction that produces vitamin D2.
Komagataella is a methylotrophic yeast within the order Saccharomycetales. It was found in the 1960s as Pichia pastoris, with its feature of using methanol as a source of carbon and energy. In 1995, P. pastoris was reassigned into the sole representative of genus Komagataella, becoming Komagataella pastoris. Later studies have further distinguished new species in this genus, resulting in a total of 7 recognized species. It is not uncommon to see the old name still in use, as of 2023; in less formal use, the yeast may confusingly be referred to as pichia.
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.
Eremothecium gossypii (also known as Ashbya gossypii) is a filamentous fungus or mold closely related to yeast, but growing exclusively in a filamentous way. It was originally isolated from cotton as a pathogen causing stigmatomycosis by Ashby and Nowell in 1926. This disease affects the development of hair cells in cotton bolls and can be transmitted to citrus fruits, which thereupon dry out and collapse (dry rot disease). In the first part of the 20th century, E. gossypii and two other fungi causing stigmatomycosis (Eremothecium coryli, Aureobasidium pullulans) made it virtually impossible to grow cotton in certain regions of the subtropics, causing severe economical losses. Control of the spore-transmitting insects - cotton stainer (Dysdercus suturellus) and Antestiopsis (antestia bugs) - permitted full eradication of infections. E. gossypii was recognized as a natural overproducer of riboflavin (vitamin B2), which protects its spores against ultraviolet light. This made it an interesting organism for industries, where genetically modified strains are still used to produce this vitamin.
Lanosterol 14α-demethylase (CYP51A1) is the animal version of a cytochrome P450 enzyme that is involved in the conversion of lanosterol to 4,4-dimethylcholesta-8(9),14,24-trien-3β-ol. The cytochrome P450 isoenzymes are a conserved group of proteins that serve as key players in the metabolism of organic substances and the biosynthesis of important steroids, lipids, and vitamins in eukaryotes. As a member of this family, lanosterol 14α-demethylase is responsible for an essential step in the biosynthesis of sterols. In particular, this protein catalyzes the removal of the C-14α-methyl group from lanosterol. This demethylation step is regarded as the initial checkpoint in the transformation of lanosterol to other sterols that are widely used within the cell.
In enzymology, a Delta24(241)-sterol reductase (EC 1.3.1.71) is an enzyme that catalyzes the chemical reaction
In enzymology, a sterol 14-demethylase (EC 1.14.13.70) is an enzyme of the Cytochrome P450 (CYP) superfamily. It is any member of the CYP51 family. It catalyzes a chemical reaction such as:
Lathosterol oxidase is a Δ7-sterol 5(6)-desaturase enzyme that in humans is encoded by the SC5D gene.
Progesterone receptor membrane component 1 is a protein which co-purifies with progesterone binding proteins in the liver and ovary. In humans, the PGRMC1 protein is encoded by the PGRMC1 gene.
Hortaea werneckii is a species of yeast in the family Teratosphaeriaceae. It is a black yeast that is investigated for its remarkable halotolerance. While the addition of salt to the medium is not required for its cultivation, H. werneckii can grow in close to saturated NaCl solutions. To emphasize this unusually wide adaptability, and to distinguish H. werneckii from other halotolerant fungi, which have lower maximum salinity limits, some authors describe H. werneckii as "extremely halotolerant".
C-5 sterol desaturase is an enzyme that is highly conserved among eukaryotes and catalyzes the dehydrogenation of a C-5(6) bond in a sterol intermediate compound as a step in the biosynthesis of major sterols. The precise structure of the enzyme's substrate varies by species. For example, the human C-5 sterol desaturase oxidizes lathosterol, while its ortholog ERG3 in the yeast Saccharomyces cerevisiae oxidizes episterol.
4α-Methylfecosterol is a metabolic intermediate of sterols made by certain fungis, can be converted to 24-Methylenelophenol by enzyme HYD1, or undergo 4-demethylation to fecosterol.
ERG11 or Sterol 14-demethylase is a fungal cytochrome P450 enzyme originally from Saccharomyces cerevisiae, belongs to family CYP51, with the CYP Symbol CYP51F1. ERG11 catalyzes the C14-demethylation of lanosterol to 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol which is the first step of biosynthesis of the zymosterol, zymosterol will be further converted into Ergosterol.
Dihydrolanosterol, or 24,25-Dihydrolanosterol, also called Lanostenol, is a sterol and the C24-25 hydrogenated products of lanosterol, dihydrolanosterol can be demethylated by mammal or yeast cytochrome P450 sterol 14alpha-demethylase.
ERG3 or sterol C-5 desaturase is a fungal enzyme originally from Saccharomyces cerevisiae, the human ortholog of ERG3 is SC5D. ERG3 localizes to both the endoplasmic reticulum and vesicles, catalyzes the C5(6)-dehydrogenation of episterol to 5-dehydroepisterol, 5-Dehydroepisterol will be further converted into ergosterol.
Cytochrome P450-DIT2 or CYP56A1 is one of the only three P450 enzyme found in fungi baker's yeast, the other two are CYP51F1(ERG11) and CYP61A1(ERG5) in the ergosterol biosynthesis pathway. CYP56A1 thought to catalyze the oxidation of tyrosine residues in the formation of L,L-dityrosine, a precursor of the spore wall.
Cytochrome P450, family 710, also known as CYP710, is a plant cytochrome P450 monooxygenase family, the proteins encoded by its family members are mainly sterol 22-desaturase, which was widely distributed in plants, and take participate in Phytosteroidogenesis. CYP710 family is considered to be the plant orthologous of fungi CYP61 family, which is lost in animal. The CYP61/CYP710 ancestor gene diverged from a gene duplication of ancestor CYP51 in early eukaryotes
ERG4 or Delta(24 )-sterol reductase or Delta(24 )-sterol reductase is an enzyme that catalyzes the last step of ergosterol biosynthesis pathway in fungi Saccharomyces cerevisiae, which 5,7,22,24(28)-ergostatetraenol converted into ergosterol.
References
- ↑ Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, et al. (October 2003). "Global analysis of protein expression in yeast". Nature. 425 (6959): 737–41. Bibcode:2003Natur.425..737G. doi:10.1038/nature02046. PMID 14562106. S2CID 4344864.
- ↑ Nelson DR (January 2018). "Cytochrome P450 diversity in the tree of life". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866 (1): 141–154. doi:10.1016/j.bbapap.2017.05.003. PMC 5681887 . PMID 28502748.
- ↑ Wilhelm BT, Marguerat S, Watt S, Schubert F, Wood V, Goodhead I, et al. (June 2008). "Dynamic repertoire of a eukaryotic transcriptome surveyed at single-nucleotide resolution". Nature. 453 (7199): 1239–43. Bibcode:2008Natur.453.1239W. doi:10.1038/nature07002. PMID 18488015. S2CID 205213499.
- ↑ Kelly SL, Lamb DC, Baldwin BC, Corran AJ, Kelly DE (April 1997). "Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents". The Journal of Biological Chemistry. 272 (15): 9986–8. doi: 10.1074/JBC.272.15.9986 . PMID 9092539.
- ↑ Chen W, Lee MK, Jefcoate C, Kim SC, Chen F, Yu JH (June 2014). "Fungal cytochrome p450 monooxygenases: their distribution, structure, functions, family expansion, and evolutionary origin". Genome Biology and Evolution. 6 (7): 1620–34. doi:10.1093/gbe/evu132. PMC 4122930 . PMID 24966179.
- ↑ Moktali V, Park J, Fedorova-Abrams ND, Park B, Choi J, Lee YH, Kang S (October 2012). "Systematic and searchable classification of cytochrome P450 proteins encoded by fungal and oomycete genomes". BMC Genomics. 13: 525. doi: 10.1186/1471-2164-13-525 . PMC 3505482 . PMID 23033934.
- ↑ Nelson DR (25 March 1999). "Note on P450 evolution in yeasts and early eukaryotes". The Cytochrome P450 Homepage. The University of Tennessee Health Science Center. 4 (1): 59–65. doi: 10.1186/1479-7364-4-1-59 . PMC 3500189 . PMID 19951895. Archived from the original on 25 October 2016.
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