Mannosylglucosaminide
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| Category | Antibiotics |
| Catalog number | BBF-02294 |
| CAS | 14510-04-4 |
| Molecular Weight | 341.31 |
| Molecular Formula | C12H23NO10 |
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Description
It is produced by the strain of Str. virginiae var. 4243-MTt1. It's an aminoglycoside antibiotic. It has anti-bacterium, mycobacterium and beer yeast effects. Trehalose does not counteract its antibacterial effect against Mycobacterium 607.
Specification
| Related CAS | 17272-81-0 (hydrochloride) |
| Synonyms | Mannosyl glucosaminide; Antibiotic 4243; 1-O-(2-Amino-2-deoxy-α-D-gluco-hexopyranosyl)-α-D-manno-hexopyranose; Mannotrehalosamine |
| IUPAC Name | (2R,3S,4S,5S,6R)-2-[(2R,3R,4R,5S,6R)-3-amino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol |
| Canonical SMILES | C(C1C(C(C(C(O1)OC2C(C(C(C(O2)CO)O)O)O)N)O)O)O |
| InChI | InChI=1S/C12H23NO10/c13-5-8(18)6(16)3(1-14)21-11(5)23-12-10(20)9(19)7(17)4(2-15)22-12/h3-12,14-20H,1-2,13H2/t3-,4-,5-,6-,7-,8-,9+,10+,11-,12-/m1/s1 |
| InChI Key | YSVQUZOHQULZQP-RYRYQYGESA-N |
Properties
| Antibiotic Activity Spectrum | Mycobacteria; Yeast |
| Solubility | Soluble in Water, Methanol |
Reference Reading
1. High efficiency of transferring a native sugar chain from a glycopeptide by a microbial endoglycosidase in organic solvents
Eri Akaike, Maki Tsutsumida, Kenji Osumi, Masaya Fujita, Takashi Yamanoi, Kenji Yamamoto, Kiyotaka Fujita Carbohydr Res. 2004 Feb 25;339(3):719-22. doi: 10.1016/j.carres.2003.12.007.
We examined the transglycosylation reaction by the recombinant endo-beta-N-acetylglucosaminidase from Mucor hiemalis (Endo-M) expressed in Candida boidinii in media containing organic solvents. The recombinant Endo-M could transglycosylate a disialo biantennary complex-type oligosaccharide from hen egg yolk glycopeptide to p-nitrophenyl N-acetyl-beta-D-glucosaminide even in the presence of 30% acetone, dimethyl sulfoxide, or methanol. The yield of the transglycosylation product reached 21-34% of the total amount of acceptor, while the yield was only about 14% in aqueous solution.
2. Hydrolases in intracellular compartments of rat liver cells. Evidence for selective activation and/or delivery
L A Casciola-Rosen, A L Hubbard J Biol Chem. 1991 Mar 5;266(7):4341-7.
We used perfused rat livers to investigate the role of endosomes versus lysosomes in the hydrolysis of endocytosed material. When perfusions were performed at 37 degrees C with 125I-asialoorosomucoid, 125I-galactosylated albumin, or 125I-mannosylated albumin, there was a 15-min lag before trichloroacetic acid-soluble degradation products were detected. Furthermore, no hydrolysis was detected at 16 degrees C, indicating that there was no significant prelysosomal degradation of these proteins. Since detection by this method depends on extensive hydrolysis, we subsequently used three small synthetic molecules from which fluorescent products are generated by a single cleavage. These were 4-methylumbelliferyl sulfate, 4-methylumbelliferyl phosphate, and 4-methylumbelliferyl-beta-D-glucosaminide, which are substrates for aryl sulfatase, acid phosphatase, and beta-hexosaminidase, respectively. Using the first two compounds, hydrolysis was detected after 3 min at 37 degrees C and still occurred, albeit to a reduced extent, at 16 and 4 degrees C. This indicates that aryl sulfatase and acid phosphatase are active prelysosomally. We found a different result with 4-methylumbelliferyl-beta-D-glucosaminide. At 37 degrees C, there was a greater than 15-min lag before hydrolysis products were measured; furthermore, hydrolysis ceased at 16 degrees C, indicating that beta-hexosaminidase is active lysosomally. Taken together, these findings show that there is selective activation and/or delivery of hydrolases along the endocytic pathway.
3. A di-N-acetylchitobiase activity is involved in the lysosomal catabolism of asparagine-linked glycoproteins in rat liver
M J Kuranda, N N Aronson Jr J Biol Chem. 1986 May 5;261(13):5803-9.
A perfused rat liver was used to study the effects of 5-diazo-4-oxo-L-norvaline on lysosomal glycoprotein catabolism. Addition of this compound (1.0 mM) to the perfusate reduced activity of beta-aspartyl-N-acetylglucosylamine amidohydrolase by 99% in 1 h. Treated livers were unable to completely degrade endocytosed N-acetyl[14C]glucosamine-labeled asialo-alpha 1-acid glycoprotein as evidenced by a 50% reduction in radiolabeled serum glycoprotein secretion compared to controls. This decreased degradation was matched by a lysosomal accumulation of glycopeptides with the structure: GlcNAc beta(1-4)GlcNAc-Asn. The result suggested the presence of an unrecognized glycosidase in rat liver lysosomes, since this remnant was extended by one more GlcNAc residue than would have been expected after specific inactivation of the amidohydrolase. Such a novel enzyme would therefore catalyze cleavage of the N-acetylglucosamine residue at the reducing end of alpha 1-acid glycoprotein oligosaccharides only following removal of the linking Asn. The activity was then detected in lysosomal extracts by using intact asialo-biantennary oligosaccharides labeled with [3H] galactose or N-acetyl[14C]glucosamine residues as a substrate. To prevent simultaneous digestion of the material from its nonreducing end, beta-D-galactosidase in the enzyme extract was first inactivated with the irreversible active site-directed inhibitor, beta-D-galactopyranosylmethyl-p-nitrophenyltriazene. The observed di-N-acetylchitobiose cleaving activity worked optimally at pH 3.4 and was uniquely associated with the lysosomal fraction of the liver homogenate. The enzyme also cleaved triantennary chains and di-N-acetylchitobiose, but failed to hydrolyze substrates that had been reduced with NaBH4. The new glycosidase was well separated from N-acetyl-beta-D-glucosaminidase (assayed with p-nitrophenyl-beta-D-glucosaminide) by gel filtration chromatography and had an apparent molecular weight of 37,000. A similar enzyme that hydrolyzes di-N-acetylchitobiose had previously been found in extracts of human liver (Stirling, J. L. (1974) FEBS Lett. 39, 171-175).
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
