Hyaluronate lyase hyaluronidase

HUGHES-INGOLD THEORY EOR SOLVENT EEEECTS ON REACTIVITY HUMMEL-DREYER TECHNIQUE HYALURONATE LYASE HYALURONIDASES HYBRIDIZATION HYDRATION ATMOSPHERE HYDRATION NUMBER Hydrazone reduction,... 

Glycopeptide-linkage hydrolases a-L-Guluronan lyase Heparin hydrolase Hyaluronate lyase Hyaluronidase L-Iduronic acid 2-sulphate sulphatase a-L-Iduronidase Inulinase Isoamylase Isopullulanase a-Lactalbumin Lactose synthase... 

Effect of Streptomyces hyaluronidase. The effects of some depolymerizing enzymes on the viscoelastic properties of proteoglycan were examined. The first example was that of Streptomyces hyaluronidase (hyaluronate lyase, EC 4.2.2.1.), which is shown as strictly specific to hyaluronic acid (j6). Thus this enzyme can degrade only the hyaluronic acid backbone of aggregate and should not attack the proteoglycan monomer. To 0.1% solution of aggregate 0.05TRU of Streptomyces hyaluronidase was added. As... 

Puhvel SM and Reisner RM (1972) The production of hyaluronidase (hyaluronate lyase) by Corynebacterium acnes. J Invest Dermatol 58 66-70 Pulverer G and Ko HL (1973) Fermentative and serological studies on Propionibacterium acnes. Appl Microbiol 25 222-229... 

Hyaluronan is widely used in applied biochemistry and enzymology as a substrate for the quantitative determination of the enzyme hyaluronidase. Scientific disputes about the possible relationship between HA and hyaluronate lyase and the pathogenicity of some streptococci are to be, as it seems, permanently carried out. Currently, much attention is paid to the study of the secondary and tertiary structures and dynamic conformation of HA in aqueous solutions and biological fluids the HA interaction with proteins, particularly receptor CD44 and other hyaladherins and the HA biocatalytic cleavage with different hyaluronidase the progression toward creating of recombinant strains and chimera products with the desired properties. 

Type 3. Microbial hyaluronidases (e.g. Streptococcus hyaluronidase). Microbial hyaluronidases hydrolyse p-N-acetylaminoglycoside bonds of a substrate and simultaneously dehydrate the residue of uronic acid at the non-reducing terminus of the molecule. Substrate specificity of bacterial hyaluronate lyases varies considerably in the different species of microbe producers. Hyaluronidase of Streptococcus pneumoniae has the highest substrate specificity it hydrolyses HA alone and does not destroy other glucosami-noglycans [43]. The hyaluronate lyase, when isolated from Streptococcus pneumoniae, reaches optimal activity at pH 6.0 with the Michaelis constant with respect to HA being equal to 3.8x 10" mol/l (in terms of Michaelis-Menten kinetics) [44]. The presence of Cd3 (about 10 mM) is necessary in order to show the maximum enzyme activity. 

In microbiologic technologies of HA production it is fragmented by the bacterial hyaluronidases that are transported into the cultural media. They are called hyaluronate lyases because they are endo-p-acetylhexosamine eliminases. The most typical representative of this class of enzymes are the Streptococcus hyaluronate lyases. The bacterial hyaluronate lyases hydrolyse endo-p-1,4-glycoside bonds in HA via the p-elimination reaction, the result of it is the formation of 4,5-unsaturated oligosaccharides of different lengths. 

The final product of the enzymatic cleavage is a 4,5-unsaturated disaccharide. Therefore, depolymerization of HA with bacterial hyaluronate lyases can be controlled not only by viscometric but also spectrophotometric methods as well. Unlike bacterial hyaluronidase, those from animal tissues are able to fragmentize HA, which could result in the production of saturated oligosaccharides. 

The hyaluronidases under consideration here have three important characteristics (1) whether they act upon choiidroitin sulfates, as well as chondroitin itself and hyaluronic acid (2) whether traiisglycosylation is a strong feature of their activity and (3) whether they catalyze the hydrolysis of an endohexosamiiiidc linjkage, or act by an intramolecular ohmination of w ater (hyaluronate lyase E.C.4.3.99.1) to produce oligosaccharides with nonreduciiig terminal unsaturated uronic acid residues of the type LIX. 

Culture filtrates from many strains of Pneumococci, Streptococci, Staphylococci, Clostridia, Proteus, and Flavobacterium show considerable hyaluronidase or hyaluronate lyase activities (Meyer et at., 1960 Gibian,... 

Hyaluronidases or hyaluronate lyases are secreted by a number of strains of bacteria, but in spite of considerable study, no direct correlation has been established between thfdr ability to secrete the enzymes and invasiveness or virulence of the organisms (-Meyer and Kapport, 1952). 

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