Glycobiology Enzymes

Bovin beta-1,4-galactosyltransferase 1 (Y289L) (Bovin B4GALT1 (Y289L)) is a mutated form of bovine-derived galactosyltransferase with a mutation at the Y289L genetic site. Bovin beta-1,4-galactosyltransferase 1 can label O-GlcNAcylated proteins with an N-azidoacetylgalactosamine (GalNAz) group. This labeling method allows for the specific, unbiased, and global labeling of O-GlcNAcylated proteins. After labeling, the appended azide group can react with a wide variety of alkyne-modified chemical probes, facilitating multiple downstream analyses.

Glucose oxidase is used in the food and beverage industry as a preservative and stabilizer and is commonly derived from the fungus Aspergillus niger. Glucose oxidase can react with intracellular glucose and oxygen (O₂) to produce hydrogen peroxide (H₂O₂) and gluconic acid, which can cut off the nutrition source of cancer cells and consequently inhibit their proliferation.

PNGase F, a glycosidase, catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. PNGase F removes nearly all N-linked oligosaccharides from glycoproteins. PNGase F can release N-glycans from glycoproteins in glycoanalytical workflows.

Endo H, Streptomyces picatus (Endo-β-N-acetylglucosaminidase H), isolated from Streptomyces plicatus, hydrolyzes the central glycosidic bond of the β1, 4-di-N-acetylchitobiose core in asparagine-linked oligosaccharides.

α-Glucosidase, Yeast (α-D-Glucosidase, Yeast), a carbohydrate hydrolyzing enzyme, catalyzes the liberation of α-glucose from the non-reducing end of the substrate. α-Glucosidase can facilitate the absorption of glucose by the small intestine. Inhibition of α-Glucosidase is an effective management of non-insulin-dependent diabetes mellitus (NIDDM).

Endo-1,3-β-glucanase (Lyticase) is an endoenzyme that can specifically cleave β-1,3-glycosidic bonds. Endo-1,3-β-glucanase recognizes and binds to β-1,3-glucan chains, catalyzing the cleavage of glycosidic bonds and hydrolyzing polysaccharides into oligosaccharides. Endo-1,3-β-glucanase eliminates vaginal Candida. Endo-1,3-β-glucanase can be used in the study of recurrent Candida vaginitis.

Endo-1,4-β-mannanase is an important catalyst that randomly cleaves the β-1,4-linkages in the main chain of mannan, releasing short-chain β-1,4-mannan and mannose. The catalytic activity of Endo-1,4-β-mannanase toward locust bean gum is enhanced by Mn²⁺, Co²⁺, Ca²⁺, Ba²⁺, Triton X-100, sodium azide and N-ethylmaleimide, completely inhibited by Hg²⁺ and N-bromosuccinimide, and partially inhibited by EDTA and Cu²⁺. Endo-1,4-β-mannanase can be used in studies related to plant hemicellulose degradation, biomass saccharification, elimination of anti-nutritional factors in feed, and manno-oligosaccharide prebiotics.

α-Rhamnosidase (α-L-Rhamnosidase) is a kind of glycoside hydrolase. α-Rhamnosidase exhibits activity against Naringin (HY-N0153), 4-NRP, flavonoid glycosides and flavanone rhamnosides, and can hydrolyze the corresponding glycosidic bonds to release L-Rhamnose (Rhamnose) (HY-N1420) and other products. α-Rhamnosidase promotes the release of total flavonoids, ginkgolides and aroma components from ginkgo tea, while also enhancing the free radical scavenging capacity of the leachate, inhibiting inflammatory cell activation and increasing its cytotoxicity against tumor cells. α-Rhamnosidase can be used in research related to bacillary dysentery and cancer.

Endo-β-N-acetylglucosaminidase (Endo S2) is a key enzyme involved in the processing of free oligosaccharides in the cytosol. Endo-β-N-acetylglucosaminidase catalyzes hydrolysis of N-linked oligosaccharides.

Urease, Jack bean is derived from jack bean and Catalyzes hydrolysis of urea to carbon dioxide and ammonia. Urease, Jack bean is useful in the determination of urea in body fluids.

Lichenase, Microorganism (endo-1,3:1,4-β-D-Glucanase) is a specific, endo-(1-3),(1-4)-β-D-glucan 4-glucanohydrolase. Lichenase, Microorganism solubilizes β-glucans from cereal grains and gives gluco-oligosaccharides (GOS). Lichenase, Microorganism can be used in the degradation of polysaccharides in the cell walls.

Neuraminidase, Microorganism (Exo-α-sialidase) is an exosialidase, is often used in biochemical studies. Neuraminidase cleaves α-ketosidic linkage between the sialic (N-acetylneuraminic) acid and an adjacent sugar residue. Neuraminidase, derived from mucosal pathogens, is a virulence factor that modifies the host's response to infection.

Invertase, baker's yeast (S. cerevisiae) is a major enzyme present in plants and microorganisms, is often used in biochemical studies. Invertase catalyzes the hydrolysis of the disaccharide sucrose into glucose and fructose.

beta-1,4-Galactosyltransferase 1 (Y285L) can enzymatic synthesis of the LacdiNAc motif. beta-1,4-Galactosyltransferase 1 (Y285L) can transfer of GalNAc from UDP-GalNAc.

β-Galactosidase, E. coli (EC 3.2.1.23; GAL) is a glycoside hydrolase that hydrolyzes the β-glycosidic bonds formed between galactose and its organic moieties. β-Galactosidase, E. coli can hydrolyze lactose to form glucose and galactose, and enter glycolysis; it can also catalyze the transgalactosylation of lactose into allolactose; allolactose can be cracked into monosaccharides.

Amyloglucosidase, Aspergillus niger (Amyloglucosidase, Aspergillus niger) is a starch-hydrolyzing enzyme with high catalytic efficiency towards soluble starch and raw starch. Amyloglucosidase, Aspergillus niger hydrolyzes α-1,4 and α-1,6 glycosidic linkages in starch and similar substrates, and primarily releases β-glucose molecules from the non-reducing ends. Amyloglucosidase, Aspergillus niger participates in glycogen metabolism and is associated with type II glycogen storage disease. Amyloglucosidase, Aspergillus niger converts starch into glucose, and is applicable to the industrial production of high-fructose syrup, ethanol and other fermented products.

PNGase F-Fast is a glycosidase that catalyzes the cleavage of internal glycosidic bonds in oligosaccharides. PNGase F-Fast removes almost all N-linked oligosaccharides from glycoproteins. PNGase F-Fast can release N-glycans from glycoproteins in the sugar analysis workflow. The cleavage site is: the glycosidic bond between the innermost N-acetylglucosamine and asparagine. PNGase F-Fast is an improved reagent that allows for rapid deglycosylation of antibodies and antibody fusions within minutes.

α-Glucosidase, bacillus stearothermophilus is a carbohydrase enzyme that catalyzes the release of α-glucose molecules. α-Glucosidase, bacillus stearothermophilus retains exoglycosidases, which hydrolyze α-glucosidic linkage at the nonreducing end of a substrate.

CMP-sialic acid synthetase (NmCSS) is an essential enzyme involved in the biosynthesis of carbohydrates and glycoconjugates containing sialic acids. CMP-sialic acid synthetase (NmCSS) activates free Sia, converting it to CMP-Sia, which is the only donor substrate for all sialyltransferases.

β-Glucosidase, almond is the rate-limiting enzyme in cellulose degradation. β-Glucosidase is a major group among glycoside hydrolases. β-Glucosidase is involved in the degradation of cellulose in soils and has potential for monitoring soil quality.