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. Author manuscript; available in PMC: 2021 Dec 18.
Published in final edited form as: J Org Chem. 2020 Nov 9;85(24):16157–16165. doi: 10.1021/acs.joc.0c02134

Table 3.

Substrate specificity study for the α2–6-sialyltransferase activity of NmSiaDW using galactosyltetrasaccharides as well as Neu5Ac, ManNAc4N3, and ManNAc6N3.

Acceptor Percentage conversion (%)
CMP-Sialic acid Transferase reaction
10 μg/mL, 10 min 3.3 mg/mL, 10 h
1 G4 aCMP-Neu5Ac (Quant.) 35±0.1 97±1
2 7N3-G4 13±1 83±1
3 9N3-G4 14±0.2 89±3
4 7NAc-G4 0 85±2
5 9NAc-G4 0 97±1
6 G4 bCMP-Neu5Ac7N3 (Quant.) 0 90±1
7 7N3-G4 0 82±2
8 9N3-G4 0 36±1
9 7NAc-G4 0 0
10 9NAc-G4 0 0
11 G4 bCMP-Neu5Ac9N3 (Quant.) 0 97±1
12 7N3-G4 0 83±2
13 9N3-G4 0 31±1
14 7NAc-G4 0 0
15 9NAc-G4 0 0

Step 1 of the reaction was carried out with aNeu5Ac, bManNAc4N3, or bManNAc6N3 (1.2 equiv.) in the presence of NmCSS (1.5 mg/mL), CTP (1 equiv.) and Tris-HCl (pH 8.5) awithout or bwith PmAldolase (4 mg/mL) and sodium pyruvate (5 equiv.).