β-elimination of hyaluronate by red king crab hyaluronidase.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
19 11 2021
19 11 2021
Historique:
received:
24
06
2021
accepted:
03
11
2021
entrez:
20
11
2021
pubmed:
21
11
2021
medline:
8
3
2022
Statut:
epublish
Résumé
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 [Formula: see text]-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.
Identifiants
pubmed: 34799594
doi: 10.1038/s41598-021-01890-3
pii: 10.1038/s41598-021-01890-3
pmc: PMC8604925
doi:
Substances chimiques
DNA, Complementary
0
Hyaluronic Acid
9004-61-9
Hyaluronoglucosaminidase
EC 3.2.1.35
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
22600Informations de copyright
© 2021. The Author(s).
Références
J Biochem. 1980 Oct;88(4):1015-23
pubmed: 7451401
Nature. 1970 Aug 15;227(5259):680-5
pubmed: 5432063
Carbohydr Res. 1972 Nov;25(1):143-52
pubmed: 4681649
Sci Rep. 2014 Mar 26;4:4471
pubmed: 24667183
Biochemistry (Mosc). 2015 Sep;80(9):1093-108
pubmed: 26555463
Biochim Biophys Acta. 2016 Apr;1860(4):661-8
pubmed: 26723173
Adv Exp Med Biol. 2017;925:75-87
pubmed: 27677277
Comp Biochem Physiol B Biochem Mol Biol. 1999 Nov;124(3):319-26
pubmed: 10631807
J Biol Chem. 1995 Feb 24;270(8):3741-7
pubmed: 7876114
Matrix. 1992 Nov;12(5):388-96
pubmed: 1484506
J Biol Chem. 1960 Apr;235:924-7
pubmed: 14417285
J Pharm Biomed Anal. 2003 Mar 10;31(3):545-50
pubmed: 12615242
PLoS One. 2014 Apr 15;9(4):e94156
pubmed: 24736576
Nature. 1957 Oct 19;180(4590):810-1
pubmed: 13483529
Chem Rev. 2006 Mar;106(3):818-39
pubmed: 16522010
Carbohydr Res. 1997 Sep 26;303(3):303-11
pubmed: 9373935
Appl Biochem Biotechnol. 2015 Oct;177(3):700-12
pubmed: 26239444
Colloids Surf B Biointerfaces. 2021 Dec;208:112095
pubmed: 34507069
PeerJ. 2020 Feb 12;8:e8579
pubmed: 32095375
J Androl. 2002 Mar-Apr;23(2):211-9
pubmed: 11868814
Biochim Biophys Acta. 1997 Feb 8;1337(2):217-26
pubmed: 9048898
Carbohydr Polym. 2017 Feb 20;158:85-92
pubmed: 28024546
Biochim Biophys Acta. 1970 Mar 18;198(3):607-9
pubmed: 5436162
J Biol Chem. 1956 Mar;219(1):13-25
pubmed: 13295251
Reg Anesth Pain Med. 2000 Sep-Oct;25(5):514-7
pubmed: 11009238
Dev Ophthalmol. 2009;44:20-25
pubmed: 19494648
Carbohydr Res. 1996 Aug 19;289:11-23
pubmed: 8805773
Biochem J. 1933;27(6):1824-8
pubmed: 16745305
J Biol Chem. 1954 Dec;211(2):605-11
pubmed: 13221568
Nucleic Acids Res. 2021 Jul 2;49(W1):W293-W296
pubmed: 33885785
Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3569-73
pubmed: 7682712
J Plast Reconstr Aesthet Surg. 2011 Jul;64(7):892-6
pubmed: 21310674
Biochem J. 1992 Apr 1;283 ( Pt 1):99-104
pubmed: 1567384
Syst Biol. 2016 Nov;65(6):997-1008
pubmed: 27121966
Plast Reconstr Surg. 2012 Apr;129(4):771e-772e
pubmed: 22456420
J Biol Chem. 1955 Oct;216(2):783-94
pubmed: 13271353
Anal Biochem. 2003 Nov 15;322(2):257-63
pubmed: 14596836
Eur J Med Res. 2016 Feb 13;21:5
pubmed: 26873038