28553-11-9

Usage

Definition

ChEBI: The beta-anomer of L-fucose 1-phosphate.

InChI:InChI=1/C6H13O8P/c1-2-3(7)4(8)5(9)6(13-2)14-15(10,11)12/h2-9H,1H3,(H2,10,11,12)/t2-,3+,4+,5-,6+/m0/s1

Upstream product

• 120449-27-6 dibenzyl-(2,3,4-tri-O-benzyl-6-deoxy-α-D-glucopyranosyl) phosphate 
• 19940-17-1 methyl 2,3,4-tri-O-acetyl-6-deoxy-α-D-glucopyranoside 
• 6087-46-3 methyl 2,3,4-tri-O-acetyl-6-chloro-6-deoxy-α-D-glucopyranoside 
• 374726-38-2 dibenzylphosphoryl 2,3,4-tri-O-acetyl-L-fucoside 
• 16741-27-8 2,3,4-tri-O-acetyl-α-L-fucopyranosyl bromide 
• 1499-17-8 o-phenylene chlorophosphate 
• 157365-62-3 2,3,4-tri-O-acetyl-6-deoxy-α-D-galactopyranose 
• 5158-64-5 2,3,4-tri-O-acetyl-D-fucopyranosyl bromide 
• 103866-94-0 C₂₇H₂₉O₈P^(2-)*2Na⁽¹⁺⁾ 
• 289901-75-3 ethyl 2,3,4-tri-O-benzoyl-6-deoxy-1-thio-β-D-glucopyranoside 
• 289901-76-4 ethyl 2,3,4-tri-O-benzyl-6-deoxy-1-thio-β-D-glucopyranoside 
• 4144-87-0 methyl 6-chloro-6-deoxy-α-D-glucopyranoside 
• 97-30-3 methyl-alpha-D-glucopyranoside 
• 488-79-9 6-deoxy-D-glucose 

Downstream Products

• 62012-79-7 dTDP-β-L-fucose 
• 30174-43-7 UDP-β-L-fucose 
• 15839-70-0 guanosine-5'-diphospho-β-L-fucose 
• 16375-63-6 UDP-6-deoxy-Gal 
• 24988-24-7 thymidine 5'-(6-deoxy-α-D-glucopyranosyl diphosphate) 
• 19083-14-8 uridine 5'-(6-deoxy-α-D-glucopyranosyl diphosphate) 

Relevant academic research and scientific papers

Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms

Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a d-galactosyl-β1-3-N-acetyl-d-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2-3-sialyltransferase or an α2-6-sialyltransferase.

Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives

Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate l-mannose in moderate yield (43%), while other l-sugars such as l-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as l-mannose.

A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity

Galactokinase (GalK), particularly GalK from Escherichia coli, has been widely employed for the synthesis of sugar-1-phosphates. In this study, a GalK from Bifidobacterium infantis ATCC 15697 (BiGalK) was cloned and over-expressed with a yield of over 80 mg/L cell cultures. The kcat/Km value of recombinant BiGalK toward galactose (164 s-1 mM -1) is 296 times higher than that of GalK from E. coli, indicating that BiGalK is much more efficient in the phosphorylation of galactose. The enzyme also exhibits activity toward galacturonic acid, which has never been observed on other wild type GalKs. Further activity assays showed that BiGalK has broad substrate specificity toward both sugars and phosphate donors. These features make BiGalK an attractive candidate for the large scale preparation of galactose-1-phosphate and derivatives.

Biochemical characterization of GDP-l-fucose de novo synthesis pathway in fungus Mortierella alpina

Mortierella alpina is a filamentous fungus commonly found in soil, which is able to produce large amount of polyunsaturated fatty acids. l-Fucose is an important sugar found in a diverse range of organisms, playing a variety of biological roles. In this study, we characterized the de novo biosynthetic pathway of GDP-l-fucose (the nucleotide-activated form of l-fucose) in M. alpina. Genes encoding GDP-d-mannose 4,6-dehydratase (GMD) and GDP-keto-6-deoxymannose 3,5-epimerase/4-reductase (GMER) were expressed heterologously in Escherichia coli. The recombinant enzymes were produced as His-tagged fusion proteins. Conversion of GDP-mannose to GDP-4-keto-6-deoxy mannose by GMD and GDP-4-keto-6-deoxy mannose to GDP-l-fucose by GMER were analyzed by capillary electrophoresis, electro-spray ionization-mass spectrometry, and nuclear magnetic resonance spectroscopy. The km values of GMD for GDP-mannose and GMER for GDP-4-keto-6-deoxy mannose were determined to be 0.77 mM and 1.047 mM, respectively. Both NADH and NADPH may be used by GMER as the coenzyme. The optimum temperature and pH were determined to be 37 °C and pH 9.0 (GMD) or pH 7.0 (GMER). Divalent cations are not required for GMD and GMER activity, and the activities of both enzymes may be enhanced by DTT. To our knowledge this is the first report on the characterization of GDP-l-fucose biosynthetic pathway in fungi.

Exploiting nucleotidylyltransferases to prepare sugar nucleotides

(Graph Presented) Enzymatic approaches to prepare sugar nucleotides are gaining in importance and offer several advantages over chemical synthesis including high yields and stereospecificity. We report the cloning, expression, and purification of two new wild-type thymidylyltransferases and observed catalysis with a wide variety of substrates. Significant product inhibition was not observed with the enzymes studied over a 24 h period, enabling the efficient preparation of 15 sugar nucleotides, clearly demonstrating the synthetic utility of these biocatalysts.

Studies on the substrate specificity of Escherichia coli galactokinase

(Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.

One-step, stereocontrolled synthesis of glycosyl 1-phosphates, uridine- 5'-diphosphogalactose, and uridine-5'-diphosphoglucose from unprotected glycosyl donors

The reaction of 2-(1,2-trans-glycopyranosyloxy)-3-methoxypyridines (MOP glycosides) with phosphoric acid leads to the corresponding 1,2-cis-1- phosphates in good yield and excellent stereoselectivity. 1-Phosphate esters of α-D-glucopyranose, α-D-galactopyranose, and 2-azido-2-deoxy-α-D- galactopyranose were thus prepared without recourse to protective groups. In the L-fucose series, the major product was the α-L-fucosyl 1-phosphate. An alternative method that relies on neighboring group participation allowed the preparation of a protected β-L-fucosyl 1-phosphate. Reaction of unprotected β-D-glucopyranosyloxy and β-D-galactopyranosyloxy MOP donors with uridine diphosphoric acid gave UDP-Glc and UDP-Gal with preponderance of the desired α-anomeric configuration.

Process for preparing nucleotide inhibitors of glycosyltransferases

Nucleotide linked 2-deoxy-2-fluoroglycosides are employed as potent competitive inhibitors of glycosyltransferases. More particularly, uridine-5'-diphospho-2-deoxy-2-fluoro-galactose (UDP-2F-Gal), guanidine-5'-diphospho-2-deoxy-2-fluoro-L-fucose (GDP-2F-Fuc), uridine-51-diphospho-2-deoxy-2-fluoro-D-glucose (UDP-2F-Glu), guanosine-5'-diphospho-2-deoxy-2-fluoro-D-mannose (GDP-2F-Man), cytosine-5'-monophospho-2-deoxy-2-fluoro-D-sialic acid, and cytosine-5'-monophospho-2-deoxy-2-KDO may be employed as inhibitors of β-1,4-galactosyltransferase, α-1,3-fucosyltransferase, glucosyltransferases, N-acetylglucosaminyltransferases, (α-mannosyltransferases, α-sialyltransferases, and KDO-transferases, respectively. Synthesis of nucleotide-linked-2-deoxy-2-fluoroglycosides is achieved using either chemoenzymatic or chemical methodologies.

Synthesis of guanosine 5′-(β-L-fucopyranosyl)-diphosphate revisited

It will be demonstrated that a successful synthesis of β-L-fucopyranose-1-phosphate (2), a key intermediate in the preparation of guanosine 5′-(β-L-fucopyranose)-diphosphate (1), strongly depends on the nature of the acyl protecting groups for the non-anomeric hydroxyl functions. Thus, the perbenzoylated, instead of peracetylated, α-L-fucopyranosyl trichloroacetimidate (11) or the corresponding ethyl β-thiofucopyranoside proved to be a convenient starting compound for the preparation of 2. Further, condensation of N,N'-dicyclohexyl-4-morpholinecarboxamidinium guanosine 5′-morpholidophosphate with excess 2 gave the title compound without concomitant formation of bisguanosine-5′-diphosphate (16).