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Literature summary for 2.3.1.78 extracted from

  • Durand, S.; Feldhammer, M.; Bonneil, E.; Thibault, P.; Pshezhetsky, A.V.
    Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC (2010), J. Biol. Chem., 285, 31233-31242.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
C123S mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer Homo sapiens
C151S mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation Homo sapiens
C305S mutation within the predicted cytosolic luminal loops, no loss of activity Homo sapiens
C308S mutation within the predicted cytosolic luminal loops, no loss of activity Homo sapiens
C374S mutation within the predicted cytosolic luminal loops, no loss of activity Homo sapiens
C434S mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer Homo sapiens
C76F mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation Homo sapiens
C79S mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation Homo sapiens
H269A complete loss of enzymic activity, intralysosomal processing is retained Homo sapiens
H451A complete loss of enzymic activity, no processing observed Homo sapiens
H605A complete loss of enzymic activity, no processing observed Homo sapiens
L208A/I209A mutation in a predicted dileucine targeting motif, mutant displays both lysosomal and plasma membrane localization Homo sapiens
additional information deletion of 12 residues at the C terminus of the enzyme, del624-635, leads to localization of the protein to the plasma membrane, in contrast to the lysosomal localization of wild-type enzyme. Mutant protein does not show maturation and has no enzymic activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome the enzyme is synthesized as a catalytically inactive 77-kDa precursor that is transported to the lysosomes via an adaptor protein-mediated pathway that involves conserved tyrosine- and dileucine-based lysosomal targeting signals in its C-terminal cytoplasmic domain with a contribution from a dileucine-based signal in the N-terminal cytoplasmic loop. In the lysosome, the precursor is cleaved into a 29-kDa N-terminal alpha-chain and a 48-kDa C-terminal beta-chain, and assembled into active 440-kDa oligomers. The subunits are held together by disulfide bonds between at least two cysteine residues, Cys123 and Cys434, in the lysosomal luminal loops of the enzyme. Homo sapiens 5764
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 x * 48000, SDS-PAGE of mature protein Homo sapiens
260000
-
 gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q68CP4 isoform 2
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification enzyme is synthesized as a catalytically inactive 77-kDa precursor that is transported to the lysosomes via an adaptor protein-mediated pathway that involves conserved tyrosine- and dileucine-based lysosomal targeting signals in its C-terminal cytoplasmic domain with a contribution from a dileucine-based signal in the N-terminal cytoplasmic loop. In the lysosome, the precursor is cleaved into a 29-kDa N-terminal alpha-chain and a 48-kDa C-terminal beta-chain, and assembled into active 440-kDa oligomers. The subunits are held together by disulfide bonds between at least two cysteine residues, Cys123 and Cys434, in the lysosomal luminal loops of the enzyme. Proteolytic cleavage may allow the nucleophile residue, His269, in the active site to access the substrate acetyl-CoA in the cytoplasm, for further transfer of the acetyl group to the terminal glucosamine on heparan sulfate Homo sapiens

Subunits

Subunits Comment Organism
oligomer x * 48000, SDS-PAGE of mature protein Homo sapiens