Functional characteristics and catalytic mechanisms of the bacterial hyaluronan synthases.
The first gene for a glycosaminoglycan synthase to be cloned was the hyaluronan (HA) synthase from S. pyogenes, which we reported in 1993. Since then, at least 20 bacterial, viral, or eukaryotic HA synthase gene or cDNA sequences and two bacterial chondroitin synthase genes have been reported. During the last decade a great deal has been elucidated about the structure, function, and mechanisms of action of the bacterial HA synthases, which are the focus of this review. Very rapid progress has been made in elucidating the mechanism of HA synthesis by the HA synthase from Pasteurella multocida. Although little of this information is applicable to understanding the mechanism of action of streptococcal HA synthases, good progress has also been made in understanding how these latter enzymes work.
Weigel
Paul H
PH
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190, USA. paul-weigel@ouhsc.edu
D002384:Catalysis; D014453:Glucuronosyltransferase / Q000378:metabolism*; D016695:Glycosyltransferases; D000076002:Hyaluronan Synthases; D008565:Membrane Proteins; D013297:Streptococcus pyogenes / Q000201:enzymology*; D014166:Transferases; D029867:Xenopus Proteins
D008565:Membrane Proteins; D029867:Xenopus Proteins; D014166:Transferases; D016695:Glycosyltransferases; D014453:Glucuronosyltransferase; C056944:HAS1 protein, Xenopus; D000076002:Hyaluronan Synthases