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J Biol Chem, Vol. 273, Issue 9, 4976-4981, February 27, 1998
From the Department of Biochemistry and Molecular Biology,
University of Oklahoma Health Sciences Center,
Oklahoma City, Oklahoma 73104
We have characterized the hyaluronan (HA)
synthase activity of the Xenopus DG42 gene product in
vitro. The recombinant enzyme produced in yeast does not possess
a nascent HA chain and, therefore, is an ideal model system for kinetic
studies of the synthase's glycosyltransferase activity. The enzymatic
rate was optimal from pH 7.6 to 8.1. Only the authentic sugar
nucleotide precursors, UDP-glucuronic acid (UDP-GlcA) and
UDP-N-acetylglucosamine (UDP-GlcNAc), were utilized to
produce a large molecular weight polymer. UDP-glucose or the galactose
epimers of the normal substrates did not substitute. The Michaelis
constant, Km, of recombinant DG42 in membranes was
60 ± 20 and 235 ± 40 µM for UDP-GlcA and
UDP-GlcNAc, respectively, which is comparable to values obtained
previously from membranes derived from vertebrate cells. The apparent
energy of activation for HA elongation is about 15 kilocalories/mol.
DG42 polymerizes HA at average rates of about 80 to 110 monosaccharides/s in vitro. The resulting HA polysaccharide
possessed molecular weights spanning 2 × 106-107 Da, corresponding to about
104 sugar residues. This is the first report characterizing
a defined eukaryotic enzyme that can produce a glycosaminoglycan.
Enzymological Characterization of Recombinant Xenopus
DG42, A Vertebrate Hyaluronan Synthase
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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