β-elimination of hyaluronate by red king crab hyaluronidase
Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its com...
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ftdoajarticles:oai:doaj.org/article:a6d32574c3b84934b4ac0d27507d6226 2023-05-15T18:06:10+02:00 β-elimination of hyaluronate by red king crab hyaluronidase Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin 2021-11-01T00:00:00Z https://doi.org/10.1038/s41598-021-01890-3 https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226 EN eng Nature Portfolio https://doi.org/10.1038/s41598-021-01890-3 https://doaj.org/toc/2045-2322 doi:10.1038/s41598-021-01890-3 2045-2322 https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226 Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) Medicine R Science Q article 2021 ftdoajarticles https://doi.org/10.1038/s41598-021-01890-3 2022-12-31T09:20:47Z Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$ β -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases. Article in Journal/Newspaper Red king crab Directory of Open Access Journals: DOAJ Articles Scientific Reports 11 1 |
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Medicine R Science Q |
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Medicine R Science Q Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin β-elimination of hyaluronate by red king crab hyaluronidase |
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Medicine R Science Q |
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Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$ β -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases. |
format |
Article in Journal/Newspaper |
author |
Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin |
author_facet |
Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin |
author_sort |
Dmitrii Sliadovskii |
title |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_short |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_full |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_fullStr |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_full_unstemmed |
β-elimination of hyaluronate by red king crab hyaluronidase |
title_sort |
β-elimination of hyaluronate by red king crab hyaluronidase |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doi.org/10.1038/s41598-021-01890-3 https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226 |
genre |
Red king crab |
genre_facet |
Red king crab |
op_source |
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) |
op_relation |
https://doi.org/10.1038/s41598-021-01890-3 https://doaj.org/toc/2045-2322 doi:10.1038/s41598-021-01890-3 2045-2322 https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226 |
op_doi |
https://doi.org/10.1038/s41598-021-01890-3 |
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Scientific Reports |
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11 |
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1766177756603744256 |