Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Streptococcus intermedius, part of the 'Streptococcus milleri group', has the ability to produce glycosaminoglycan depolymerising enzymes (hyaluronidase and chrondroitin sulphate depolymerase) which is unique amongst the viridans streptococci and may contribute to their virulence in brain and liver abscesses. The growth of S. intermedius strain UNS 35 was studied in basal medium supplemented with chondroitin sulphate A (CS-A, sulphated at position 4 of the N-acetylgalactosamine moiety) or chondroitin sulphate C (CS-C, sulphated at position 6 of the N-acetylgalactosamine moiety) as the major carbohydrate source. CS-A but not CS-C supported the growth of S. intermedius. Extracellular degradation of CS-A resulted in the initial accumulation of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyluronic acid)-D-galactose (deltaUA GalNAc-0S), and low levels of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyl uronic acid)-4-O-sulpho-D-galactose (deltaUA GalNAc-4S) in the medium with GalNAc-0S being subsequently utilised during bacterial growth. Metabolic end-products included formate and ethanol but not lactate, indicating that growth was probably carbon-limited. The CS-A contained 30% CS-C, which was also depolymerised resulting in the formation of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyluronic acid)-6-O-sulpho-D-galactose (deltaUA GalNAc-6S) in the culture supernate, but this unsaturated disaccharide was apparently not utilised during growth. The results indicate that S. intermedius produced CS-AC depolymerase, which was inducible and extracellular, and sulphatase activity. Experiments with authentic deltaUA GalNAc-4S and deltaUA GalNAc-6S demonstrated that deltaUA GalNAc4S rather than deltaUA GalNAc-6S was the preferred substrate for the sulphatase. Therefore, it is suggested that the CS-AC depolymerase of S. intermedius may play a role in the destruction of CS in host tissues, facilitating bacterial spread, and also in bacterial nutrition by the liberation of nutrients at the site of infection.
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PMID:Degradation and utilisation of chondroitin sulphate by Streptococcus intermedius. 863 52

Using the transglycosylation reaction of testicular hyaluronidase, reconstructions of hybrid glycosaminoglycans (GAGs) containing 6-sulfated (GalNAc6S), 4-sulfated (GalNAcS) and unsulfated N-acetylgalactosamine (GalNAc) were investigated. First, chondroitin 4-sulfate (Ch4S) as a donor containing GalNAc4S and the pyridylaminated (PA) chondroitin 6-sulfate (Ch6S) hexasaccharide as an acceptor containing GalNAc6S were subjected to transglycosylation reaction. Second, when the resulting PA-Ch6S(hexa-)-Ch4S(di-)octasaccharide and chondroitin (Ch) were used as an acceptor and as a donor containing GalNAc, respectively, a new decasaccharide having a hybrid structure composed of disaccharide units derived from Ch6S, Ch4S and Ch was reconstructed. Using a systematic combination of each donor and acceptor molecule, it was possible to reconstruct various types of hybrid GAGs.
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PMID:Enzymatic reconstruction of a hybrid glycosaminoglycan containing 6-sulfated, 4-sulfated, and unsulfated N-acetylgalactosamine. 1032 56

A method was developed for the reconstruction of glycosaminoglycan (GAG) oligosaccharides using the transglycosylation reaction of an endo-beta-N-acetylhexosaminidase, testicular hyaluronidase, under optimal conditions. Repetition of the transglycosylation using suitable combinations of various GAGs as acceptors and donors made it possible to custom-synthesize GAG oligosaccharides. Thus we prepared a library of chimeric GAG oligosaccharides with hybrid structures composed of disaccharide units such as GlcA-GlcNAc (from hyaluronic acid), GlcA-GalNAc (from chondroitin), GlcA-GalNAc4S (from chondroitin 4-sulfate), GlcA-GalNAc6S (from chondroitin 6-sulfate), IdoA-GalNAc (from desulfated dermatan sulfate), and GlcA-GalNAc4,6-diS (from chondroitin sulfate E). The specificity of the hyaluronidase from Streptococcus dysgalactiae (hyaluronidase SD) was then investigated using these chimeric GAG oligosaccharides as model substrates. The results indicate that the specificity of hyaluronidase SD is determined by the following restrictions at the nonreducing terminal side of the cleavage site: (i) at least one disaccharide unit (GlcA-GlcNAc) is necessary for the enzymatic action of hyaluronidase SD; (ii) cleavage is inhibited by sulfation of the N-acetylgalactosamine; (iii) hyaluronidase SD releases GlcA-GalNAc and IdoA-GalNAc units as well as GlcA-GlcNAc. At the reducing terminal side of the cleavage site, the sulfated residues on the N-acetylgalactosamines in the disaccharide units were found to have no influence on the cleavage. Additionally, we found that hyaluronidase SD can specifically and endolytically cleave the internal unsulfated regions of chondroitin sulfate chains. This demonstration indicates that custom-synthesized GAG oligosaccharides will open a new avenue in GAG glycotechnology.
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PMID:Chimeric glycosaminoglycan oligosaccharides synthesized by enzymatic reconstruction and their use in substrate specificity determination of Streptococcus hyaluronidase. 1073 64