Complementary characterization of a hyaluronic acid splitting enzyme from Streptococcus agalactiae.
A hyaluronic acid splitting enzyme of Streptococcus agalactiae was characterized by splitting mechanism, Michaelis-constant and inhibition type for sulfated hyaluronic acid: The enzyme splits hyaluronic acid as a hyaluronate lyase [EC 4.2.2.1]. The Km = 8 x 10(-4) mg ml-1 was determined with the influence of substrate inhibition constant Kiu = 2 x 10(-6) mg ml-1. Sulfated hyaluronic acid inhibits the enzyme in a partially non-competitive way. The inhibition constant is Ki = 5.47 x 10(-4) mg ml-1. The GBS-hyaluronate lyase cleaves hyaluronic acid as an endoglycosidase. The work is related with the intention to establish a hyaluronate lyase of microbial origin as a therapeutical enzyme replacing bovine hyaluronidase.
Rodig
H
H
Hans-Knöll-Institut für Naturstoff-Forschung e.V., Jena, Germany.
Ozegowski
J H
JH
Peschel
G
G
Müller
P J
PJ
D000818:Animals; D002417:Cattle; D002845:Chromatography / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D006820:Hyaluronic Acid / Q000378:metabolism*; D007700:Kinetics; D011133:Polysaccharide-Lyases / Q000378:metabolism*; D013292:Streptococcus agalactiae / Q000201:enzymology*
D006820:Hyaluronic Acid; D011133:Polysaccharide-Lyases; C100002:hyaluronate lyase