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InterPro: IPR015882 Beta-N-acetylhexosaminidase-like

Protein matches Help

UniProtKB

Matches:

605 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR015882 HexNAc-like_b

Secondary

IPR001540

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02838	Glyco_hydro_20b	605
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001540 Glycoside hydrolase, family 20

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004563 beta-N-acetylhexosaminidase activity

InterPro annotation

Entry Details in BioMart

Abstract

Glycoside hydrolase family 20 GH20 comprises enzymes with several known activities; beta-hexosaminidase (EC:3.2.1.52); lacto-N-biosidase (EC:3.2.1.140). Carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base in this family of enzymes.

In the brain and other tissues, beta-hexosaminidase A degrades GM2 gangliosides; specifically, the enzyme hydrolyses terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer, with one alpha, one beta-A and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; and hexosaminidase S is a homodimer of alpha chains. The two beta chains are derived from the cleavage of a precursor. Mutations in the beta-chain lead to Sandhoff disease, a lysosomal storage disorder characterised by accumulation of GM2 ganglioside [1].

This entry represents the beta-N-acetylhexosaminidase-like domain. It contains a similar fold but lacks the catalytic centre.

Structural links Help

PDB - click here

SCOP: d.92.2.1

CATH: 3.20.20.80 , 3.30.379.10

Database links Help

Enzyme: EC:3.2.1.52

PANDIT: PF02838

Taxonomic coverage Help

Example proteins Help

P06865 Beta-hexosaminidase subunit alpha

P20060 Beta-hexosaminidase subunit beta

Q22492 Beta-hexosaminidase A

Q54468 Chitobiase

Q8WSF3 Probable beta-hexosaminidase fdl

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR013812	Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain
IPR012291	Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR004867	Glycoside hydrolase, family 20, C-terminal
IPR014756	Immunoglobulin E-set
IPR015883	Glycoside hydrolase, family 20, catalytic core
IPR008965	Carbohydrate-binding
IPR015882	Beta-N-acetylhexosaminidase-like
IPR004866	Carbohydrate-binding, chitobiase/hexosaminidase-type, N-terminal
IPR017853	Glycoside hydrolase, catalytic core
IPR001540	Glycoside hydrolase, family 20
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Bolhuis PA, Ponne NJ, Bikker H, Baas F, Vianney de Jong JM. Molecular basis of an adult form of Sandhoff disease: substitution of glutamine for arginine at position 505 of the beta-chain of beta-hexosaminidase results in a labile enzyme. Biochim. Biophys. Acta 1182 142-6 1993 [PubMed: 8357844] http://dx.doi.org/10.1016/0925-4439(93)90134-M

Additional Reading Open in usermanual
	Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W. The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease. J. Mol. Biol. 328 2003 669-81 [PubMed: 12706724] http://dx.doi.org/10.1016/S0022-2836(03)00311-5
	Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, James MN. Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327 2003 1093-109 [PubMed: 12662933] http://dx.doi.org/10.1016/S0022-2836(03)00216-X
	Schuette CG, Weisgerber J, Sandhoff K. Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS. Glycobiology 11 2001 549-56 [PubMed: 11447134] http://dx.doi.org/10.1093/glycob/11.7.549
	Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB. Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J. Mol. Biol. 300 2000 611-7 [PubMed: 10884356] http://dx.doi.org/10.1006/jmbi.2000.3906
	Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3 1996 638-48 [PubMed: 8673609] http://dx.doi.org/10.1038/nsb0796-638
	Lemieux MJ, Mark BL, Cherney MM, Withers SG, Mahuran DJ, James MN. Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis. J. Mol. Biol. 359 2006 913-29 [PubMed: 16698036] http://dx.doi.org/10.1016/j.jmb.2006.04.004

InterPro 23.1