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5.
Figure 4

Figure 4. 19F-NMR spectra obtained for the reaction mixture containing Z-[3-F]PEP, ManNAc, MnCl2 and C. jejuni NeuNAc synthase. From: Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni.

Signal at −140 p.p.m. is from Z-[3-F]PEP and the signal at −199.4 p.p.m. is from the product (3S)-[3-F]NeuNAc.

Appavu K. Sundaram, et al. Biochem J. 2004 October 1;383(Pt 1):83-89.
6.
Figure 3

Figure 3. 1H-NMR spectra of NeuNAc. From: Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni.

1H-NMR spectra of (a) NeuNAc, (b) (3R)-[3-2H]NeuNAc obtained from E-[3-2H]PEP, and (c) (3S)-[3-2H]NeuNAc obtained from Z-[3-2H]PEP. Only the regions exhibiting signals for C-3 protons are shown (the signal at 1.78 p.p.m. is from Ha and the signal at 2.19 p.p.m. is from Heq). The signal at 2 p.p.m. is from the methyl group of N-acyl side chain.

Appavu K. Sundaram, et al. Biochem J. 2004 October 1;383(Pt 1):83-89.
7.
Figure 5

Figure 5. 19F-NMR spectra obtained for the reaction mixture containing E- and Z-[3-F]PEP (3:2 mixture), ManNAc, MnCl2 and C. jejuni NeuNAc synthase. From: Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni.

The signal at −140 p.p.m. is from Z-[3-F]PEP and the signal at −150 p.p.m. is from E-[3-F]PEP. The signal at −199.4 p.p.m. is from the product (3S)-[3-F]NeuNAc (formed from the Z-isomer).

Appavu K. Sundaram, et al. Biochem J. 2004 October 1;383(Pt 1):83-89.

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