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. Author manuscript; available in PMC: 2012 Oct 5.
Published in final edited form as: Bioconjug Chem. 2009 Mar 18;20(3):608–618. doi: 10.1021/bc800534r

Table 1.

The catalytic activities of the wild-type α3Gal-T with Ser347, and mutants of α3Gal-T enzymes at different lactose concentrations with each sugar nucleotides, UDP-Gal and UDP-GalNAc.

Donor substrates
Enzyme UDP-Gal UDP-GalNAc
20 mmol lac
(%)		 200 mmol lac
(%)		 20 mmol lac
(%)		 200 mmol lac
(%)
α1,3 GalT 280HAA282 (WT) 100 100 N/A N/A
α1,3 GalT 280AAA282 14 41 4 6
α1,3 GalT 280GAG282 5 27 0.3 2
α1,3 GalT 280AGG282 0.4 1 3 19
α1,3 GalT 280SGG282 5 5 2 11
α1,3 GalT 280TGG282 3 15 1 6
α1,3 GalT 280LGG282 2 1 3 2
α1,3 GalT 280VGG282 4 16 0.5 3

The 100% specific activity of the wild type (WT) is 1.100 ±0.20 pmol/ng/min.