Reference : A novel three-enzyme reaction cycle for the synthesis of N-acetyllactosamine with in sit...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/17344
A novel three-enzyme reaction cycle for the synthesis of N-acetyllactosamine with in situ regeneration of uridine 5'-diphosphate glucose and uridine 5'-diphosphate galactose
English
Zervosen, Astrid mailto [Université de Liège - ULg > > Centre de recherches du cyclotron >]
Elling, Lothar [> > > >]
1996
Journal of the American Chemical Society
American Chemical Society
118
8
1836-1840
Yes (verified by ORBi)
International
0002-7863
1520-5126
Washington
DC
[en] LacNAc ; in situ regeneration ; enzymatic synthesis
[fr] beta-1,4-galactosyltransferase ; alpha-2,6-sialyltransferase
[en] A new three-enzyme reaction cycle consisting of sucrose synthase, UDP glucose 4‘-epimerase, and human β-1,4-galactosyltransferase was established for the synthesis of N-acetyllactosamine (LacNAc) with in situ regeneration of UDP galactose. We found that UDP glucose 4‘-epimerase is reductively inactivated in the presence of UMP and acceptor substrates of β-1,4-galactosyltransferase. Reactivation of UDP glucose 4‘-epimerase by the transition state analogues dUDP or dTDP 6-deoxy-d-xylo-4-hexulose in combination with the repetitive batch technique enabled us to use the native enzymes for 11 days in this cycle. With 10 U of sucrose synthase, 5 U of UDP glucose 4‘-epimerase, and 1.25 U of β-1,4-galactosyltransferase, 594 mg of LacNAc could be synthesized. N-Acetyllactosamine was also subsequently converted to Neu5Acα2,6Galβl,4GlcNAc with α-2,6-sialyltransferase and CMP-Neu5Ac.
http://hdl.handle.net/2268/17344
10.1021/ja953495e

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