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beta N-acetyl hexosaminidase alpha chain (hexosaminidase-A, HEXA)

Function: - responsible for the degradation of GM2 gangliosides, & a variety of other molecules containing terminal N-acetyl hexosamines, in the brain & other tissues - hydrolysis of terminal non-reducing N-acetyl- D-hexosamine residues in N-acetyl-beta-D-hexosaminides - form B is active against certain oligosaccharides - form S has no measurable activity Structure: - belongs to the glycosyl hydrolase 20 family - 3 forms of beta-hexosaminidase: a) hexosaminidase A is a trimer composed of - one alpha chain, - one beta-A chain - one beta-B chain b) hexosaminidase B is a tetramer of - two beta-A - two beta-B chains c) hexosaminidase S is an homodimer of - two alpha chains - two beta chains are derived from the cleavage of a precursor chain - N-linked glycan at Asn-115 consists of Man(3)-GlcNAc(2) Compartment: lysosome Pathology: - defects in HEXA are the cause of Tay-Sachs disease Laboratory: - HEXA gene mutation - HEXA gene deletion

Related

beta-N-acetylhexosaminidase A in dried blood spot beta-N-acetylhexosaminidase A in fibroblasts beta-N-acetylhexosaminidase A in leukocytes beta-N-acetylhexosaminidase A+beta-N-acetylhexosaminidase A.total in leukocytes beta-N-acetylhexosaminidase A+beta-N-acetylhexosaminidase A.total in serum beta-N-acetylhexosaminidase A/beta-N-acetylhexosaminidase A.total in serum

General

glycoprotein protein subunit

Properties

SIZE: entity length = 529 aa MW = 61 kD COMPARTMENT: lysosome MOTIF: signal sequence {1-22} cysteine residue {C58} MODIFICATION: cysteine residue {C104} cysteine residue {C104} MODIFICATION: cysteine residue {C58} N-glycosylation site {N115} N-glycosylation site {N157} cysteine residue {C277} MODIFICATION: cysteine residue {C328} N-glycosylation site {N295} glutamate residue {E323} cysteine residue {C328} MODIFICATION: cysteine residue {C277} cysteine residue {C505} MODIFICATION: cysteine residue {C522} cysteine residue {C522} MODIFICATION: cysteine residue {C505}

Database Correlations

OMIM correlations MORBIDMAP 606869 UniProt P06865 KEGG correlations ENZYME 3.2.1.52

References

  1. UniProt :accession P06865
  2. HEXAdb; HEXA mutation database http://www.hexdb.mcgill.ca/?Topic=HEXAdb
  3. Genedis; note=Tay Sachs disease website http://life2.tau.ac.il/Genedis/Tables/Tay_Sachs/tay_sachs.html
  4. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=HEXA

Component-of

beta N-acetylhexosaminidase