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106864-00-0

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106864-00-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 106864-00-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,6,8,6 and 4 respectively; the second part has 2 digits, 0 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 106864-00:
(8*1)+(7*0)+(6*6)+(5*8)+(4*6)+(3*4)+(2*0)+(1*0)=120
120 % 10 = 0
So 106864-00-0 is a valid CAS Registry Number.

106864-00-0Relevant articles and documents

Biosynthesis of UDP-glucuronic acid and UDP-galacturonic acid in Bacillus cereus subsp. cytotoxis NVH 391-98

Broach, Bryan,Gu, Xiaogang,Bar-Peled, Maor

, p. 100 - 112 (2012)

The food borne pathogen Bacillus cereus produces uronic acid-containing glycans that are secreted in a shielding biofilm environment, and certain alkaliphilic Bacillus deposit uronate-glycan polymers in the cell wall when adapting to alkaline environments. The source of these acidic sugars is unknown and, in the present study, we describe the functional identification of an operon in Bacillus cerues subsp. cytotoxis NVH 391-98 that comprises genes involved in the synthesis of UDP-uronic acids in Bacillus spp. Within the operon, a UDP-glucose 6-dehydrogenase converts UDP-glucose in the presence of NAD+ to UDP-glucuronic acid and NADH, and a UDP-GlcA 4-epimerase (UGlcAE) converts UDP-glucuronic acid to UDP-galacturonic acid. Interestingly, in vitro, both enzymes can utilize the TDP-sugar forms as well, albeit at lower catalytic efficiency. Unlike most of the very few bacterial 4-epimerases that have been characterized, which are promiscuous, the B. cereus UGlcAE enzyme is very specific and cannot use UDP-glucose, UDP-N-acetylglucosamine, UDP-N-acetylglucosaminuronic acid or UDP-xylose as substrates. Size exclusion chromatography suggests that UGlcAE is active as a monomer, unlike the dimeric form of plant enzymes; the Bacillus UDP-glucose 6-dehydrogenase is also found as a monomer. Phylogenic analysis further suggests that the Bacillus UGlcAE may have evolved separately from other bacterial and plant epimerases. Our results provide insight into the formation and function of uronic acid-containing glycans in the lifecycle of B. cereus and related species containing homologous operons, as well as a basis for determining the importance of these acidic glycans. We also discuss the ability to target UGlcAE as a drug candidate.

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Neufeld et al.

, p. 4430 (1958)

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The presence of an uronic acid epimerase in a strain of pneumococcus type I.

SMITH,MILLS,BERNHEIMER,AUSTRIAN

, p. 640 - 641 (1958)

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Improved one-pot multienzyme (OPME) systems for synthesizing UDP-uronic acids and glucuronides

Muthana, Musleh M.,Qu, Jingyao,Xue, Mengyang,Klyuchnik, Timofey,Siu, Alex,Li, Yanhong,Zhang, Lei,Yu, Hai,Li, Lei,Wang, Peng G.,Chen, Xi

supporting information, p. 4595 - 4598 (2015/05/27)

Arabidopsis thaliana glucuronokinase (AtGlcAK) was cloned and shown to be able to use various uronic acids as substrates to produce the corresponding uronic acid-1-phosphates. AtGlcAK or Bifidobacterium infantis galactokinase (BiGalK) was used with a UDP-sugar pyrophosphorylase, an inorganic pyrophosphatase, with or without a glycosyltransferase for highly efficient synthesis of UDP-uronic acids and glucuronides. These improved cost-effective one-pot multienzyme (OPME) systems avoid the use of nicotinamide adenine dinucleotide (NAD+)-cofactor in dehydrogenase-dependent UDP-glucuronic acid production processes and can be broadly applied for synthesizing various glucuronic acid-containing molecules. This journal is

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