Welcome to LookChem.com Sign In|Join Free

CAS

  • or

18546-17-3

Post Buying Request

18546-17-3 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

18546-17-3 Usage

Uses

D-Fuculose is a aldohexose sugar and an epimer of D-Fucose (F836120).

Check Digit Verification of cas no

The CAS Registry Mumber 18546-17-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,8,5,4 and 6 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 18546-17:
(7*1)+(6*8)+(5*5)+(4*4)+(3*6)+(2*1)+(1*7)=123
123 % 10 = 3
So 18546-17-3 is a valid CAS Registry Number.

18546-17-3Relevant articles and documents

Characterization of a novel D-arabinose isomerase from Thermanaeromonas toyohensis and its application for the production of D-ribulose and L-fuculose

Iqbal, Muhammad Waheed,Riaz, Tahreem,Hassanin, Hinawi A.M.,Ni, Dawei,Mahmood Khan, Imran,Rehman, Abdur,Mahmood, Shahid,Adnan, Muhammad,Mu, Wanmeng

, (2019/09/30)

D-Ribulose and L-fuculose are potentially valuable rare sugars useful for anticancer and antiviral drugs in the agriculture and medicine industries. These rare sugars are usually produced by chemical methods, which are generally expensive, complicated and do not meet the increasing demands. Furthermore, the isomerization of D-arabinose and L-fucose byDD-arabinose and L-fucose by D-arabinose isomerase from bacterial sources for the production of D-ribulose and L-fuculose have not yet become industrial due to the shortage of biocatalysts, resulting in poor yield and high cost of production. In this study, a thermostable D-ribulose- and L-fuculose producing D-arabinose isomerase from the bacterium Thermanaeromonas toyohensis was characterized. The recombinant D-arabinose isomerase from T. toyohensis (Thto-DaIase) was purified with a single band at 66 kDa using His-trap affinity chromatography. The native enzyme existed as a homotetramer with a molecular weight of 310 kDa, and the specific activities for both D-arabinose and L-fucose were observed to be 98.08 and 85.52 U mg?1, respectively. The thermostable recombinant Thto-DaIase was activated when 1 mM Mn2+ was added to the reactions at an optimum pH of 9.0 at 75 °C and showed approximately 50% activity for both D-arabinose and L-fucose at 75 °C after 10 h. The Michaelis-Menten constant (Km), the turnover number (kcat) and catalytic efficiency (kcat/Km) for D-arabinose/L-fucose were 111/81.24 mM, 18,466/10,688 min?1, and 166/132 mM?1 min?1, respectively. When the reaction reached to equilibrium, the conversion rates of D-ribulose from D-arabinose and L-fuculose from L-fucose were almost 27% (21 g L?1) and 24.88% (19.92 g L?1) from 80 g L?1 of D-arabinose and L-fucose, respectively.

Molecular characterization of a thermostable l-fucose isomerase from Dictyoglomus turgidum that isomerizes l-fucose and d-arabinose

Hong, Seung-Hye,Lim, Yu-Ri,Kim, Yeong-Su,Oh, Deok-Kun

experimental part, p. 1926 - 1934 (2012/09/22)

A recombinant thermostable l-fucose isomerase from Dictyoglomus turgidum was purified with a specific activity of 93 U/mg by heat treatment and His-trap affinity chromatography. The native enzyme existed as a 410 kDa hexamer. The maximum activity for l-fucose isomerization was observed at pH 7.0 and 80 °C with a half-life of 5 h in the presence of 1 mM Mn2+ that was present one molecular per monomer. The isomerization activity of the enzyme with aldose substrates was highest for l-fucose (with a kcat of 15,500 min-1 and a Km of 72 mM), followed by d-arabinose, d-altrose, and l-galactose. The 15 putative active-site residues within 5 A of the substrate l-fucose in the homology model were individually replaced with other amino acids. The analysis of metal-binding capacities of these alanine-substituted variants revealed that Glu349, Asp373, and His539 were metal-binding residues, and His539 was the most influential residue for metal binding. The activities of all variants at 349 and 373 positions except for a dramatically decreased kcat of D373A were completely abolished, suggesting that Glu349 and Asp373 were catalytic residues. Alanine substitutions at Val131, Met197, Ile199, Gln314, Ser405, Tyr451, and Asn538 resulted in substantial increases in Km, suggesting that these amino acids are substrate-binding residues. Alanine substitutions at Arg30, Trp102, Asn404, Phe452, and Trp510 resulted in decreases in kcat, but had little effect on Km.

Conversion of l-rhamnose into ten of the sixteen 1- and 6-deoxyketohexoses in water with three reagents: d-tagatose-3-epimerase equilibrates C3 epimers of deoxyketoses

Gullapalli, Pushpakiran,Yoshihara, Akihide,Morimoto, Kenji,Rao, Devendar,Akimitsu, Kazuya,Jenkinson, Sarah F.,Fleet, George W.J.,Izumori, Ken

supporting information; experimental part, p. 895 - 898 (2010/05/03)

The efficient isomerization of l-rhamnose [the only cheaply available deoxy hexose] to 1-deoxy-l-psicose, 1-deoxy-d-psicose, 1-deoxy-l-fructose, 1-deoxy-d-fructose, 1-deoxy-l-tagatose, 6-deoxy-l-psicose, 6-deoxy-d-psicose, 6-deoxy-l-fructose, 6-deoxy-d-fructose, and 6-deoxy-l-tagatose is described. The conversion of rhamnose to ten of the sixteen 1- and 6-deoxyketohexoses is accomplished in water in three steps. The range of substrates for d-tagatose-3-epimerase (DTE) is extended to 1- and 6-deoxyketoses. An authentic sample of 6-deoxy-d-psicose is prepared from d-psicose.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 18546-17-3