Hyaluronidases

Meyer, Karl; Rapport, Maurice M.

doi:10.1002/9780470122587.ch6

Cited by 48 publications

(41 citation statements)

References 161 publications

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“…4, 5) closely resembles the (β/α) 8 TIM barrel of the parent BVHyal structure. The number of sheets constituting the central part of the TIM barrel varies, however, but is similar to that of various forms of the BVHyal structures.…”

Section: Description Of the Model Structuresmentioning

confidence: 96%

“…The modeled C-terminal domain was obtained using the ab initio method and its primary, secondary, or tertiary structure is not similar to any other molecule's sequence of 3D domain structure currently available, which implies a novel fold and possibly novel function. A characteristic (β/α) 8 TIM barrel fold of the main domain, which is the catalytic domain that supports the binding to the substrate, and its hydrolytic degradation by means of double-displacement, retaining mechanism (described in The molecule is sown in similar orientation and using the same color scheme and labeling as that of Hyal-1 in Fig. 4 A- The catalytic H-donor (acid) Glu131, in red, is shown in position to interact with the C1 carbon.…”

Section: Supplementary Materialsmentioning

confidence: 99%

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Hyaluronidases: Their Genomics, Structures, and Mechanisms of Action

2006

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Section: Description Of the Model Structuresmentioning

confidence: 96%

Section: Supplementary Materialsmentioning

confidence: 99%

Hyaluronidases: Their Genomics, Structures, and Mechanisms of Action

2006

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“…Substrate HA oligosaccharide Reaction products (%) (GlcUA-GlcNAc) 2 (GlcUA-GlcNAc) 2 100 (GlcUA-GlcNAc) 3 (GlcUA-GlcNAc) 3 100 (GlcUA-GlcNAc) 4 (GlcUA-GlcNAc) 2 46.8 (GlcUA-GlcNAc) 3 32.7 (GlcUA-GlcNAc) 4 20.5 (GlcUA-GlcNAc) 5 (GlcUA-GlcNAc) 2 31.5 (GlcUA-GlcNAc) 3 48.3 (GlcUA-GlcNAc) 4 14.7 (GlcUA-GlcNAc) 5 5.50 charide were detected in the reaction mixture. A longer reaction time decreased the amount of octasaccharide and increased the amounts of tetrasaccharide and hexasaccharide (Fig.…”

Section: Products Of Hydrolysis By Bth Of Ha Oligosaccharidesmentioning

confidence: 99%

“…Bovine testicular hyaluronidase (BTH) (hyaluronoglucosaminidase; EC 3.2.1.35) is an endo-b-N-acetyl-d-hexosaminidase that hydrolyzes hyaluronan (HA) at the b1,4-N-acetylglucosaminide bonds [N-acetylglucosamine (GlcNAc)b-(1 fi 4)-glucuronic acid (GlcUA)] [1][2][3][4]. In addition, the enzyme also hydrolyzes chondroitin sulfates at the b-1,4-N-acetylgalactosaminide bonds, N-acetylgalactosamine (GalNAc)b-(1 fi 4)-GlcUA, but at a lower efficiency, which is dependent on the structure of the chondroitin sulfate [1,5].…”

Section: Introductionmentioning

confidence: 99%

Mechanism for the hydrolysis of hyaluronan oligosaccharides by bovine testicular hyaluronidase

Kakizaki¹,

Ibori²,

Kojima

et al. 2010

The FEBS Journal

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Synthetic hyaluronan oligosaccharides with defined structures and their pyridylaminated derivatives were used to investigate the mechanism of hydrolysis of hyaluronan by bovine testicular hyaluronidase. The products of the hydrolysis were analyzed by HPLC and ion‐spray mass spectroscopy (MS). It was confirmed that the minimum substrate for bovine testicular hyaluronidase is the hyaluronan hexasaccharide, even though it is a poor substrate that is barely cleaved, even on prolonged incubation. When hyaluronan octasaccharide was the substrate, increasing amounts of tetrasaccharide and hexasaccharide were produced with increasing time of incubation. Whereas disaccharide was not detectable in the reaction mixture by HPLC, MS analysis revealed trace amounts. The data suggest that the enzyme generates a disaccharide intermediate from hyaluronan oligosaccharide, the majority of which is transferred to the nonreducing ends of other oligosaccharides, only traces being released as free disaccharide. When hyaluronan octasaccharide, with an unsaturated glucuronic acid at the nonreducing end, was used as a substrate, only a tetrasaccharide was detected by HPLC. However, MS showed that the product was a mixture of equal amounts of two tetrasaccharides, one with and the other without the unsaturated glucuronic acid. This suggests that, in the case of substrates with a double bond at the nonreducing end, a tetrasaccharide is cleaved off instead of a disaccharide. The results of the experiments with pyridylaminated oligosaccharides were entirely consistent with these conclusions, and in addition showed the importance of the reducing end of the substrate for the enzyme to recognize the length of the saccharide.

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“…Hyaluronidase (hyaluronoglucosaminidase; EC 3.2.1.35) is an endo-b-N-acetyl-D-hexosaminidase that hydrolyzes HA at the b1,4-N-acetylglucosaminide bonds [GlcNAc-b-1 ! 4)-(GlcUA)] [3][4][5][6] . Besides that, the enzyme also hydrolyzes Ch/ Ch4S/Ch6S/DS at the b-1,4-N-acetylgalactosaminide bonds [GalNAc-b1 !…”

Section: Introductionmentioning

confidence: 99%