Disease relevance of Rhodotorula

• Various species of "Streptomyces," "Aspergillus," "Rhodotorula," "Brevilegnia," "Syncephalastrum," and "Stysanus" were found to transform precocene II to three major metabolites [1].
• Cloning, sequencing and expression in E. coli of a D-amino acid oxidase cDNA from Rhodotorula gracilis active on cephalosporin C [2].
• We describe two cases of fungemia caused by Trichosporon beigelii and Rhodotorula glutinis respectively in two neutropenic patients with hematological malignancies who were treated with amphotericin B [3].
• Endocarditis caused by Rhodotorula successfully treated with 5-fluorocytosine [4].
• Under intensive aeration (1.3 l/l min) the associated growth of Rhodotorula rubra GED2 and Lactobacillus casei subsp. casei in cheese whey ultrafiltrate (55 g lactose/l) proceeded effectively for both cultures with production of maximum carotenoids (12.4 mg/l culture fluid) [5].

High impact information on Rhodotorula

• An mRNA-type intron is present in the Rhodotorula hasegawae U2 small nuclear RNA gene [6].
• The flavoenzyme d-amino acid oxidase (DAAO) from Rhodotorula gracilis is a peroxisomal enzyme and a prototypical member of the glutathione reductase family of flavoproteins [7].
• We report here the isolation, purification, and characterization of a catalytically active cytosolic 10 S multienzyme complex for triacylglycerol biosynthesis from Rhodotorula glutinis during exponential growth [8].
• Influence of moderate temperatures on myristoyl-CoA metabolism and acyl-CoA thioesterase activity in the psychrophilic antarctic yeast Rhodotorula aurantiaca [9].
• Arg(285), one of the very few conserved residues in the active site of d-amino acid oxidases, has been mutated to lysine, glutamine, aspartate, and alanine in the enzyme from the yeast Rhodotorula gracilis (RgDAAO) [10].

Chemical compound and disease context of Rhodotorula

• A red yeast, Rhodotorula, an infrequent cause of infection in humans, was isolated from a patient with acute myeloblastic leukemia undergoing bone marrow transplant while he received parenteral nutritional fluids by an indwelling catheter [11].

Biological context of Rhodotorula

• Nucleotide sequence of gene for phenylalanine ammonia-lyase from Rhodotorula rubra [12].
• In the yeast Rhodotorula glutinis, accumulation of the tetraphenylphosphonium ion (TPP+) was increased under conditions of osmotic stress, indicating a hyperpolarization of the negative membrane potential (delta psi) [13].
• Altered nutrient content (levels of glucose) caused a drastic reduction in cell growth and triacylglycerol (TAG) production in the wild-type (WT) Rhodotorula glutinis [14].
• We have developed a serum-free in vitro system consisting of RPMI 1640 supplemented with one of three fatty acids (arachidonic, linoleic, or linolenic) that supports consistent and reproducible molting to the fourth larval stage in the presence of a basidiomycetous yeast, Rhodotorula minuta [15].
• Kinetics of D-glucose and 2-deoxy-D-glucose transport by Rhodotorula glutinis [16].

Anatomical context of Rhodotorula

• Microbodies were observed in cells of Sporobolomyces roseus strain Y and Rhodotorula glutinis strain CY when grown on methane but rarely when grown on glucose [17].
• Analysis of the saturation isotherm revealed the presence of a one-carrier system for L-glucose in the plasma membrane of Rhodotorula glutinis [18].
• Glucosamine and chitin accumulation in cell walls of the yeast Rhodotorula glutinis CBS 3044. Influence of culture conditions [19].

Associations of Rhodotorula with chemical compounds

• Maximal enzyme activity in Rhodotorula glutinis (2 units/g, wet weight, of yeast) was induced in late-log phase (12 to 14 hours) of growth in a culture medium containing 1.0% malt extract, 0.1% yeast extract, and 0.1% L-phenylalanine [20].
• The yeast Rhodotorula pilimanae produces the dihydroxamate siderophore rhodotorulic acid (RA) in prodigious amounts when starved for iron [21].
• Substitution of nucleoside triphosphates for ascorbate in the thymine 7-hydroxylase reaction of Rhodotorula glutinis [22].
• The turnover numbers at infinite substrate and oxygen concentrations were: 20,700/4,250 and 1,730/360 ([2-1H]/[2-2H]alanine and valine, respectively) for the Rhodotorula and 3,150/440 and 2,500/520 ([2-1H]/[2-2H]alanine and valine, respectively) for the Trigonopsis enzymes [23].
• Cell-free preparations from Rhodotorula glutinis catalyzed the conversion of deoxyribonucleosides to ribonucleosides in a pyrimidine deoxyribonucleoside 2' -hydroxylase reaction [24].

Gene context of Rhodotorula

• Glutamate-alpha-ketoadipate transaminase, saccharopine reductase, and saccharopine dehydrogenase activities were demonstrated in extracts of Rhodotorula glutinis but alpha-aminoadipate reductase activity could not be measured in whole cells or in extracts [25].
• Cytochrome P-450-dependent catabolism of triethanolamine in Rhodotorula mucilaginosa [26].
• D-Amino-acid oxidase from Rhodotorula gracilis was irreversibly inactivated by phenylglyoxal in a biphasic process [27].
• To evaluate this hypothesis, the cDNA encoding the highly active DAAO from the red yeast Rhodotorula gracilis was mutated to remove the carboxy-terminal peroxisomal targeting sequence [28].
• Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme [29].

Analytical, diagnostic and therapeutic context of Rhodotorula

• Limited proteolysis and site-directed mutagenesis reveal the origin of microheterogeneity in Rhodotorula gracilis D-amino acid oxidase [30].
• The l-mandelate dehydrogenase (L-MDH) from the yeast Rhodotorula graminis is a mitochondrial flavocytochrome b2 which catalyses the oxidation of mandelate to phenylglyoxylate coupled with the reduction of cytochrome c. We have used the N-terminal sequence of the enzyme to isolate the gene encoding this enzyme using the PCR [31].
• After developing a rapid gel filtration method to prepare pure and stable apoenzyme forms of D-amino acid oxidase from the yeast Rhodotorula gracilis, we carried out comparative kinetic studies on the reconstitution to holoenzyme (with FAD) of the intact (40 kDa) and proteolyzed (38.3 kDa) apoenzyme forms of this oxidase [32].
• Dissection of the structural determinants involved in formation of the dimeric form of D-amino acid oxidase from Rhodotorula gracilis: role of the size of the betaF5-betaF6 loop [33].
• Batch and fed-batch carotenoid production by Rhodotorula glutinis-Debaryomyces castellii co-cultures in corn syrup [34].

References