streptomyces

Streptomyces A-Factor is a microbial hormone found in Streptomyces griseus. A-factor triggers streptomycin biosynthesis and cell differentiation by binding a repressor-type receptor protein (ArpA) and dissociating it from DNA.

Erythromycin (E-Mycin) is a Macrolide and Macrolide Antimicrobial. The physiologic effect of erythromycin is by means of Decreased Sebaceous Gland Activity.

Fervenulin is isolated from a nematicidal actinomycete Streptomyces sp. CMU-MH021 with nematicidal activity. It also inhibits egg hatch and J2 mortality of M. incognita (MICs: 30 μg/mL and 120 μg/mL, respectively).

Streptomyces pepsin inhibitor is used as a pepsin inhibitor.

Nikkomycin Z (Nikkomycin Z from Streptomyces tendae) is a competitive chitin synthase inhibitor.It inhibitor of the growth of filamentous fungi, insects, acarids and yeasts.

exo-β-1,3-Xylosidase, Streptomyces sp. SWU10 (EC.3.2.1.72), is an endo-xylanase capable of degrading xylan into various xylooligosaccharides.

Aminopeptidase I, Streptomyces griseus (EC 3.4.11.22), exhibits broad substrate specificity, effectively removing N-terminal residues from most proteins, except when the penultimate residue is an imino acid. Aminopeptidase I contains two Zn2+ binding sites.

Sphingomyelinase, Streptomyces sp. (EC 3.1.4.12), is a hydrolase enzyme involved in sphingolipid metabolism. It belongs to the DNase I superfamily and catalyzes the breakdown of sphingomyelin (SM) into phosphocholine and ceramide.

Pectin methylesterase, Streptomyces avermitilis (EC 3.1.1.11), catalyzes the hydrolysis of pectin methyl esters to produce pectic acid and methanol.

Protease, Streptomyces griseus, exhibits broad substrate specificity with its active site composed of aspartate, histidine, and serine residues. It predominantly hydrolyzes peptide bonds on the carboxyl side of glutamic acid or aspartic acid.

Phospholipase A2, derived from Streptomyces violaceoruber (EC 3.1.1.4), hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Its primary substrates include phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogs. It can also hydrolyze phosphatidylinositol and phosphatidylserine. Phospholipase A2 effectively targets phospholipids within intact cell membranes by specifically recognizing and catalyzing the hydrolysis of the sn-2 acyl bond, resulting in the release of arachidonic acid and lysophospholipids.

Hyaluronidase, derived from Streptomyces hyalurolyticus (EC 3.2.1.35), is capable of degrading hyaluronic acid. This enzyme randomly cleaves the β-N-acetylhexosamine-[1→4] glycosidic bonds found in hyaluronic acid, chondroitin, and chondroitin sulfate.

Cholesterol Oxidase from Streptomyces sp. (EC 1.1.3.6) is a monomeric flavoprotein containing FAD that catalyzes the initial step in cholesterol catabolism. This bifunctional enzyme first oxidizes cholesterol to cholest-5-en-3-one in an FAD-dependent reaction, then isomerizes it to cholest-4-en-3-one, releasing H2O2 in the process.

Mutanolysin from Streptomyces globisporus ATCC 21553 is an N-acetylmuramidase that can cleave bacterial cell wall polymer peptidoglycan at the β-N-acetylmuramoyl-(1→4)-N-acetylglucosamine linkage. The carboxy-terminal region of mutanolysin plays a role in recognizing and binding unique cell wall polymers.

Chitosanase, derived from *Streptomyces griseus* (EC 3.2.1.132), catalyzes the endohydrolysis of β(1,4) glycosidic bonds between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Additionally, chitosanase, from the same source, is capable of hydrolyzing chitosan and carboxymethyl cellulose.

Labiase, derived from Streptomyces fulvissimus TU-6, is an enzyme preparation capable of lysing various gram-positive bacteria, including Lactobacillus, Pediococcus, and Streptococcus species. Labiase exhibits both β-N-acetyl-D-glucosaminidase and lysozyme activities.

Glycerokinase, Streptomyces canus (EC 2.7.1.30), is a phosphotransferase involved in the synthesis of triglycerides and glycerophospholipids. It catalyzes the MgATP-dependent phosphorylation of glycerol, producing sn-glycerol-3-phosphate and serves as the rate-limiting enzyme in glycerol utilization.

Alkalophilic Proteinase, Streptomyces sp is a biocatalyst and a crucial enzyme in new biocatalyst technology. Enzyme engineering focuses on improving reaction kinetics, substrate selectivity, and activity under harsh conditions (e.g., low or high pH). By incorporating stimulus responsiveness into these enzyme modifications, dynamic control over activity is also achieved.

Blasticidin S HCl is a natural product and an inhibitor of protein synthesis. Blasticidin S HCl is a broad-spectrum antibiotic that can inhibit the cell growth of prokaryotes, fungi, plants and mammalian cells.

Ionomycin is a calcium ion carrier and an antibiotic that binds to calcium ions (Ca2+). The main function of Ionomycin is to induce cellular responses by increasing the intracellular calcium ion concentration. In experiments, Ionomycin is typically used to activate calcium-dependent processes, such as apoptosis and enzyme activity.

Bekanamycin (Kanamycin B) is an aminoglycoside antibiotic extracted from Streptomyces kanamyceticus, which inhibits a range of Gram-positive and Gram-negative bacteria.

6-Diazo-5-oxo-L-nor-Leucine (DON) is a glutamine antagonist, an irreversible glutaminolysis inhibitor (Ki=6 μM) with antitumor (particularly pancreatic cancer), antibacterial, and antiviral activities.

Ascamycin is a 5'-O-sulfonamide ribonucleoside antibiotic produced by Streptomyces spp. It exhibits selective antibacterial activity against Xanthomonas species, inhibiting Xanthomonas citri, Xanthomonas oryzae, and phage with MIC values of 0.4 μg/mL, 12.5 μg/mL, and 12.5 μg/mL respectively.

Reticulol is an isocoumarin derivative produced by certain species of Streptomyces. Reticulol inhibits cAMP phosphodiesterase (IC50 = 41 µM). Recticulol (M.W. 222.2) exhibits a potent in vitro cytotoxicity against the human lung tumor cell line A427 and the mouse melanoma cell line B16F10.