A Facile Enzymatic Synthesis of Uridine Diphospho-[14C]galacturonic Acid

Basu, Subhash; Dotson, Garry D.; Raetz, Christian R. H.

doi:10.1006/abio.2000.4479

Cited by 20 publications

(10 citation statements)

References 22 publications

(15 reference statements)

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“…Formation of uronic acids was detected using 2 U GAO / mg of substrate [28,35], 100 U GAO /mg of substrate [38], and by varying reaction times, leading to conversions and yields as high as 95% and 90%, respectively [37,38].…”

Section: Further Oxidation To Uronic Acidmentioning

confidence: 99%

“…Aldehydes produced through GAO oxidation of mono-and oligosaccharides can be further oxidized to corresponding uronic acids [26,31,[35][36][37][38] (Scheme 1, F). Formation of uronic acids was detected using 2 U GAO / mg of substrate [28,35], 100 U GAO /mg of substrate [38], and by varying reaction times, leading to conversions and yields as high as 95% and 90%, respectively [37,38].…”

Section: Further Oxidation To Uronic Acidmentioning

confidence: 99%

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Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Parikka

Master

Tenkanen

2015

Journal of Molecular Catalysis B: Enzymatic

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Section: Further Oxidation To Uronic Acidmentioning

confidence: 99%

Section: Further Oxidation To Uronic Acidmentioning

confidence: 99%

Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Parikka

Master

Tenkanen

2015

Journal of Molecular Catalysis B: Enzymatic

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“…This material was redissolved in 1 ml of H 2 O. The concentration was calculated using the UDP extinction coefficient of 9.9 ϫ 10 3 M Ϫ1 cm Ϫ1 at 262 nm (29). Before NMR analysis could be performed on the above UDPGlcNAc3N sample, the excess triethylamine was removed with a Dowex AG-50W 8X column.…”

Section: Large Scale Purification Of the Product Synthesized In Vitro Bymentioning

confidence: 99%

Oxidation and Transamination of the 3″-Position of UDP-N-Acetylglucosamine by Enzymes from Acidithiobacillus ferrooxidans

Sweet

Ribeiro

Raetz

2004

Journal of Biological Chemistry

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Lipid A, a major component of the outer membranes of Escherichia coli and other Gram-negative bacteria, is usually constructed around a ␤-1,6-linked glucosamine disaccharide backbone. However, in organisms like Acidithiobacillus ferrooxidans, Leptospira interrogans, Mesorhizobium loti, and Legionella pneumophila, one or both glucosamine residues are replaced with the sugar 2,3-diamino-2,3-dideoxy-D-glucopyranose. We now report the identification of two proteins, designated GnnA and GnnB, involved in the formation of the 2,3-diamino-2,3-dideoxy-D-glucopyranose moiety. The genes encoding these proteins were recognized because of their location between lpxA and lpxB in A. ferrooxidans. Based upon their sequences, the 313-residue GnnA protein was proposed to catalyze the NAD ؉ -dependent oxidation of the glucosamine 3-OH of UDP-GlcNAc, and the 369-residue GnnB protein was proposed to catalyze the subsequent transamination to form UDP 2-acetamido-3-amino-2,3-dideoxy-␣-D-glucopyranose (UDP-GlcNAc3N). Both gnnA and gnnB were cloned and expressed in E. coli using pET23c؉. In the presence of L-glutamate and NAD ؉ , both proteins were required for the conversion of [␣-32 P]UDPGlcNAc to a novel, less negatively charged sugar nucleotide shown to be [␣-32 P]UDP-GlcNAc3N. The latter contained a free amine, as judged by modification with acetic anhydride. Using recombinant GnnA and GnnB, ϳ0.4 mg of the presumptive UDP-GlcNAc3N was synthesized. The product was purified and subjected to NMR analysis to confirm the replacement of the GlcNAc 3-OH group with an equatorial NH 2 . As shown in the accompanying papers (Sweet, C.

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“…Substrates for GO include dihydroxyacetone, raffinose, melibiose, lactose, guar gum, galactose, and its derivatives as galactosamine and methyl-galactopyranosides (Whittaker, 2002;Mazur, 1991;Chiu et al, 1996). Applications of GO include determination of Dgalactose and lactose concentrations (Tkac et al, 2000;Karube et al, 1990); enzymatic synthesis of carbohydrates (Franke et al, 2003;Andreana et al, 2002;Basu et al, 2000;Liu and Dordick, 1999;Mazur, 1991); histochemical staining studies (Schulte and Spicer, 1983;Roberts and Gupta, 1965); biotransformation of glycobiopolymers into paper strength additives (Chiu et al, 1996); and early detection of colon cancer by a cytochemical staining method used to identify a dissacharide (Gal-β(1,3)-GalNAc) expressed in the rectal mucus (Vucenik et al, 2001;Carter et al, 1997;Said et al, 1999). One problem associated with the use of GO regards the availability of sufficiently pure enzyme.…”

Section: Introductionmentioning

confidence: 99%

Production and characterization of galactose oxidase produced by four isolates of Fusarium graminearum

Gasparotto

Abrão

Inagaki

et al. 2006

Braz. arch. biol. technol.

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A screening aimed to find new galactose oxidase producer isolates and to evaluate the production among Fusarium graminearum strains was conducted. Thirty-five isolates out of 39 analysed produced the enzyme at several levels. The data indicated a wide distribution of galactose oxidase within F. graminearum and also revealed new producer isolates. The enzyme produced by different isolates showed similar thermal activity and stability and were active on same substrates. However, the optimum pH ranged from 7.0 to 7.5. Thus, all evaluated isolates were suitable for the production of galactose oxidase.

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A Facile Enzymatic Synthesis of Uridine Diphospho-[14C]galacturonic Acid

Cited by 20 publications

References 22 publications

Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Oxidation and Transamination of the 3″-Position of UDP-N-Acetylglucosamine by Enzymes from Acidithiobacillus ferrooxidans

Production and characterization of galactose oxidase produced by four isolates of Fusarium graminearum

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