Changing the donor cofactor of bovine α1, 3-galactosyltransferase by fusion with UDP-galactose 4-epimerase: more efficient biocatalysis for synthesis of α-Gal …

X Chen, Z Liu, J Wang, J Fang, H Fan… - Journal of Biological …, 2000 - ASBMB
Two fusion enzymes consisting of uridine diphosphogalactose 4-epimerase (UDP-galactose
4-epimerase, EC 5.1. 3.2) and α1, 3-galactosyltransferase (EC 2.4. 1.151) with an N-terminal
His 6 tag and an intervening three-glycine linker were constructed by in-frame fusion of the
Escherichia coli galEgene either to the 3′ terminus (f1) or to the 5′ terminus (f2) of a
truncated bovine α1, 3-galactosyltransferase gene, respectively. Both fusion proteins were
expressed in cell lysate as active, soluble forms as well as in inclusion bodies as improperly …
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