Allantoin is a chemical compound with formula C4H6N4O3. It is also called 5-ureidohydantoin or glyoxyldiureide. It is a diureide of glyoxylic acid. Allantoin is a major metabolic intermediate in most organisms including animals, plants and bacteria. It is produced from uric acid, which itself is a degradation product of nucleic acids, by action of urate oxidase (uricase).
Streptomyces is the largest genus of Actinobacteria and the type genus of the family Streptomycetaceae. Over 500 species of Streptomyces bacteria have been described. As with the other Actinobacteria, streptomycetes are gram-positive, and have genomes with high GC content. Found predominantly in soil and decaying vegetation, most streptomycetes produce spores, and are noted for their distinct "earthy" odor that results from production of a volatile metabolite, geosmin.
Streptomyces clavuligerus is a species of Gram-positive bacterium notable for producing clavulanic acid.
All microorganisms, with a few exceptions, have highly conserved DNA sequences in their genome that are transcribed and translated to efflux pumps. Efflux pumps are capable of moving a variety of different toxic compounds out of cells, such as antibiotics, heavy metals, organic pollutants, plant-produced compounds, quorum sensing signals, bacterial metabolites and neurotransmitters via active efflux, which is vital part for xenobiotic metabolism. This active efflux mechanism is responsible for various types of resistance to bacterial pathogens within bacterial species - the most concerning being antibiotic resistance because microorganisms can have adapted efflux pumps to divert toxins out of the cytoplasm and into extracellular media.
Doxorubicin (DXR) is a 14-hydroxylated version of daunorubicin, the immediate precursor of DXR in its biosynthetic pathway. Daunorubicin is more abundantly found as a natural product because it is produced by a number of different wild type strains of streptomyces. In contrast, only one known non-wild type species, streptomyces peucetius subspecies caesius ATCC 27952, was initially found to be capable of producing the more widely used doxorubicin. This strain was created by Arcamone et al. in 1969 by mutating a strain producing daunorubicin, but not DXR, at least in detectable quantities. Subsequently, Hutchinson's group showed that under special environmental conditions, or by the introduction of genetic modifications, other strains of streptomyces can produce doxorubicin. His group has also cloned many of the genes required for DXR production, although not all of them have been fully characterized. In 1996, Strohl's group discovered, isolated and characterized dox A, the gene encoding the enzyme that converts daunorubicin into DXR. By 1999, they produced recombinant Dox A, a Cytochrome P450 oxidase, and found that it catalyzes multiple steps in DXR biosynthesis, including steps leading to daunorubicin. This was significant because it became clear that all daunorubicin producing strains have the necessary genes to produce DXR, the much more therapeutically important of the two. Hutchinson's group went on to develop methods to improve the yield of DXR, from the fermentation process used in its commercial production, not only by introducing Dox A encoding plasmids, but also by introducing mutations to deactivate enzymes that shunt DXR precursors to less useful products, for example baumycin-like glycosides. Some triple mutants, that also over-expressed Dox A, were able to double the yield of DXR. This is of more than academic interest because at that time DXR cost about $1.37 million per kg and current production in 1999 was 225 kg per annum. More efficient production techniques have brought the price down to $1.1 million per kg for the non-liposomal formulation. Although DXR can be produced semi-synthetically from daunorubicin, the process involves electrophilic bromination and multiple steps and the yield is poor. Since daunorubicin is produced by fermentation, it would be ideal if the bacteria could complete DXR synthesis more effectively.
Aminocoumarin is a class of antibiotics that act by an inhibition of the DNA gyrase enzyme involved in the cell division in bacteria. They are derived from Streptomyces species, whose best-known representative – Streptomyces coelicolor – was completely sequenced in 2002. The aminocoumarin antibiotics include:
Streptomyces coelicolor is a soil-dwelling Gram-positive bacterium that belongs to the genus Streptomyces.
Methylenomycin A is a cyclopentanone derived antibiotic produced by Streptomyces coelicolor A3(2) that is effective against both Gram-negative and Gram-positive bacteria. Methylenomycins are naturally produced in two variants: A and B.
Methylenomycin B is a cyclopentanone derived antibiotic produced by Streptomyces coelicolor A3(2) that is effective against both Gram-negative and Gram-positive bacteria. Methylenomycins are naturally produced in two variants: A and B.
In molecular biology, the ABM domain is a protein domain that is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species, which can carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The structure of ActVA-Orf6 monooxygenase from Streptomyces coelicolor, which is involved in actinorhodin biosynthesis, reveals a dimeric alpha+beta barrel topology. There is also a conserved histidine that is likely to be an active site residue. In the S. coelicolor protein SCO1909 this domain occurs as a repeat.
Geosmin synthase or germacradienol-geosmin synthase designates a class of bifunctional enzymes that catalyze the conversion of farnesyl diphosphate (FPP) to geosmin, a volatile organic compound known for its earthy smell. The N-terminal half of the protein catalyzes the conversion of farnesyl diphosphate to germacradienol and germacrene D, followed by the C-terminal-mediated conversion of germacradienol to geosmin. The conversion of FPP to geosmin was previously thought to involve multiple enzymes in a biosynthetic pathway.
Terpentedienyl-diphosphate synthase is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction
Streptomyces isolates have yielded the majority of human, animal, and agricultural antibiotics, as well as a number of fundamental chemotherapy medicines. Streptomyces is the largest antibiotic-producing genus of actinobacteria, producing chemotherapy, antibacterial, antifungal, antiparasitic drugs, and immunosuppressants. Streptomyces isolates are typically initiated with the aerial hyphal formation from the mycelium.
Streptomyces albofaciens is a bacterium species from the genus of Streptomyces which produces oxytetracycline, spiramycin, albopeptin A, albopeptin B and alpomycin.
Streptomyces diastatochromogenes is a bacterium species from the genus of Streptomyces. Streptomyces diastatochromogenes produces polyketomycin, concanamycin A, concanamycin B, concanamycin C, momofulvenone A, azdimycin, toyocamycin and oligomycins.
Streptomyces griseolus is a bacterium species from the genus of Streptomyces which has been isolated from soil. Streptomyces griseolus produces complex antifungal antibiotics like oligomycins and the antibiotics anisomycin and sinefungin.
The Citrate-Mg2+:H+ (CitM) / Citrate-Ca2+:H+ (CitH) Symporter (CitMHS) Family (TC# 2.A.11) is a family of transport proteins belonging to the Ion transporter superfamily. Members of this family are found in Gram-positive and Gram-negative bacteria, archaea and possibly eukaryotes. These proteins all probably arose by an internal gene duplication event. Lensbouer & Doyle (2010) have reviewed these systems, classifying the porters with three superfamilies, according to ion-preference:
Streptomyces virginiae is a bacterium species from the genus of Streptomyces which has been isolated from soil. Streptomyces virginiae produces actithiazic acid, virginiamycins and cycloserine.
s-SodF RNA is a non-coding RNA (ncRNA) molecule identified in Streptomyces coelicolor. It is produced from sodF mRNA by cleavage of about 90 nucleotides from its 3′UTR. However it does not affect the function of sodF mRNA, but It acts on another mRNA called sodN. s-SodF RNA has a sequence complementary to sodN mRNA from the 5′-end up to the ribosome binding site. It pairs with sodN mRNA, blocks its translation and facilitates sodN mRNA decay. In Streptomyces sodF and sodN genes produce FeSOD and NiSOD superoxide dismutases containing Fe and Ni respectively. Their expression is inversely regulated by nickel-specific Fur-family regulator called Nur. When Ni is present Nur directly represses sodF transcription, and indirectly induces sodN.
Cytochrome P450, family 105, also known as CYP105, is a cytochrome P450 monooxygenase family in bacteria, predominantly found in the phylum Actinobacteria and the order Actinomycetales. The first three genes and subfamilys identified in this family is the herbicide-inducible P-450SU1 and P-450SU2 from Streptomyces griseolus and choP from Streptomyces sp 's cholesterol oxidase promoter region.
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