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Information on EC 2.3.1.78 - heparan-alpha-glucosaminide N-acetyltransferase and Organism(s) Homo sapiens and UniProt Accession Q68CP4
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2.3.1.78 heparan-alpha-glucosaminide N-acetyltransferaseIUBMB Comments
Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed. Also acts on heparin. Not identical with EC 2.3.1.3 glucosamine N-acetyltransferase or EC 2.3.1.4 glucosamine-phosphate N-acetyltransferase.
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Word Map
- 2.3.1.78
- lysosomal
- mucopolysaccharidosis
-
sanfilippo
- glycosaminoglycans
- naglu
- alpha-n-acetylglucosaminidase
- medicine
-
sulfamidase
- n-acetylglucosamine-6-sulfatase
-
splice-site
-
facies
-
nonsyndromic
- pigmentosa
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
hgsnat, acetyl-coa:alpha-glucosaminide n-acetyltransferase, heparan-alpha-glucosaminide n-acetyltransferase, tmem76, transmembrane protein 76, acetyl-coenzyme a:alpha-glucosaminide n-acetyltransferase, heparan sulfate acetyl-coa alpha-glucosaminide n-acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-CoA:alpha-glucosaminide N-acetyltransferase
-
-
-
-
acetyl-coenzyme A-alpha-glucosaminide N-acetyltransferase
-
-
-
-
acetyltransferase, alpha-glucosaminide
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:heparan-alpha-D-glucosaminide N-acetyltransferase
Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed. Also acts on heparin. Not identical with EC 2.3.1.3 glucosamine N-acetyltransferase or EC 2.3.1.4 glucosamine-phosphate N-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
79955-83-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine
CoA + 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-N-acetyl-beta-D-glucosamine
i.e. fluorescent BODIPY-glucosamine
-
-
?
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-beta-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + BODIPY-beta-D-glucosaminide
CoA + BODIPY-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
acetyl-CoA + 4-methylumbelliferyl beta-D-glucosaminide
?
-
substrate activity assay
-
-
?
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-beta-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + glucosamine-L-iduronic acid-D-glucosamine
?
-
reduced with NaBH4
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
acetyl-CoA + heparin alpha-D-glucosaminide
CoA + heparin N-acetyl-D-glucosamine
-
also acetylates di- and tetrasaccharide fragments of heparin
-
-
?
acetyl-CoA + phosphatidylethanolamine
CoA + N-acetylphosphatidylethanolamine
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + beta-D-glucosamine
CoA + N-acetyl-beta-D-glucosamine
-
-
-
?
acetyl-CoA + beta-D-glucosamine
CoA + N-acetyl-beta-D-glucosamine
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
initial step in heparan sulfate degradation
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency causes mucopolysaccharidosis type IIIC
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
initial step in heparan sulfate degradation
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency causes mucopolysaccharidosis type IIIC
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
D-glucosamine
substrate 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine, pH 6.5, 37°C
0.28
D-glucosamine
substrate 4-methylumbelliferyl-beta-D-glucosaminide, pH 6.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000017
-
leukocyte, substrate 4-methylumbelliferyl-alpha-D-glucosaminide + acetyl-CoA
0.000022
-
leukocyte, substrate 4-methylumbelliferyl-beta-D-glucosaminide + acetyl-CoA
0.000058
-
fibroblast, substrate 4-methylumbelliferyl-beta-D-glucosaminide + acetyl-CoA
0.000059
-
fibroblast, substrate 4-methylumbelliferyl-alpha-D-glucosaminide + acetyl-CoA
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is present in the lysosomal membranes purified from the normal human skin fibroblasts, but absent in those from the skin fibroblasts of patients with mucopolysaccharidosis IIIC
-
from primary skin fibroblasts, wild-type SF4528 and KD8, and MPS IIIC mutants thereof
-
deficiency on leukocytes from patients with Sanfillippo syndrome type C
additional information
-
immortalization of cell lines, the cells retain the mucopolysaccharidosis type IIIC phenotype, overview
-
deficiency on fibroblasts from patients with Sanfillippo syndrome type C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
HGSNAT coimmunoprecipitates with antibodies to ALIX, which is associated with the endosomal sorting complexes required for transport proteins
additional information
-
enzyme is associated to detergent-resistent microdomains of lysosomal membrane
-
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.
-
enzyme is acetylated at the cytoplasmic side of the lysosome and the acetyl group is then transferred to the inside where it is used to acetylate heparan sulfate
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network. A mutation within the V-domain of ALIX demonstrates enhanced HGSNAT association. HGSNAT still coimmunoprecipitates with truncations of ALIX lacking the V-domain. Knockdown of ALIX does not inhibit HGSNAT trafficking through the endo-lysosomal network
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HGNAT_HUMAN
663
12
73293
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67000
-
all missense mutants have a smaller molecular mass of ca. 67 kDa, determined by SDS-PAGE and Western blot analysis
77000
77000
-
the four polymorphisms, mutant P237Q, V481L, K523Q and A615T, determined by SDS-PAGE and Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
two major bands are detected by SDS-PAGE, 12000 Da (catalytic subunit) and 145000 Da
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C123S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer
C151S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
C305S
mutation within the predicted cytosolic luminal loops, no loss of activity
C308S
mutation within the predicted cytosolic luminal loops, no loss of activity
C374S
mutation within the predicted cytosolic luminal loops, no loss of activity
C434S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer
C76F
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
C79S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
H269A
complete loss of enzymic activity, intralysosomal processing is retained
L208A/I209A
mutation in a predicted dileucine targeting motif, mutant displays both lysosomal and plasma membrane localization
A489E
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
A615T
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
C76F
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
D562V
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
E471K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
G262R
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
G424S
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
K523Q
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
L137P
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
M482K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
N273K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
P237Q
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
P283L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
P571L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
R344C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
R344H
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S518F
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S539C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S541L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
V481L
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
W403C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
additional information
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
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
additional information
mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network
additional information
-
mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network
additional information
-
c.1-1925_118+296del, mutation, 2339-bp deletion including exon 1
additional information
-
c.1030C>T, missense mutation, predicted effect on protein, p.R344C
additional information
-
c.1209G>T, missense mutation, predicted effect on protein, p.W403C
additional information
-
c.1271dupG, mutation, predicted effect on protein, p.I425HfsX45
additional information
-
c.1411G>A, missense mutation, predicted effect on protein, p.E471K
additional information
-
c.1441G>T, polymorphism, predicted effect on protein, p.V481L
additional information
-
c.1457G>A, missense mutation, predicted effect on protein, p.G486E
additional information
-
c.1466C>A, missense mutation, predicted effect on protein, p.A489E
additional information
-
c.1516C>T, nonsense mutation, predicted effect on protein, p.R506X, premature termination codon
additional information
-
c.1553C>T, missense mutation, predicted effect on protein, p.S518F
additional information
-
c.1622C>T, missense mutation, predicted effect on protein, p.S541L
additional information
-
c.1674C>G, nonsense mutation, predicted effect on protein, p.Y558X, premature termination codon
additional information
-
c.1843G>A, polymorphism, predicted effect on protein, p.A615T
additional information
-
c.410T>C, missense mutation, predicted effect on protein, p.L137P
additional information
-
c.641delG, mutation, predicted effect on protein, p.Gly214AspfsX62
additional information
-
c.739delA, mutation, predicted effect on protein, p.R247GfsX29
additional information
-
c.848C>T, missense mutation, predicted effect on protein, p.P283L
additional information
-
c.887C>A, nonsense mutation, predicted effect on protein, p.S296X, premature termination codon
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from transfected COS-7 cells by ion-exchange chromatography on a Mono Q HR 5/5 column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytogenetic analysis of skin fibroblast cell lines derived from enzyme-deficient mutant parent cell line and immortalized cell lines
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
medicine
analysis
direct method to assay HGSNAT enzymatic activity using fluorescent BODIPY-glucosamine, i.e. 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine, as a substrate
analysis
direct method to assay HGSNAT enzymatic activity using fluorescent BODIPY-glucosamine as a substrate. The assay is specific and potentially applicable for the biochemical diagnosis of mucopolysaccharidosis III type and high-throughput screening for HGSNAT inhibitors
medicine
direct method to assay HGSNAT enzymatic activity using fluorescent BODIPY-glucosamine, i.e. 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine, as a substrate. Cultured fibroblasts of mucopolysaccharidosis III type C patients show a profound deficiency of HGSNAT activity as compared to normal controls as well as to mucopolysaccharidosis III type A and D patients known to have normal HGSNAT activity
medicine
identification of HGSNAT mutations in six patients with non-syndromic retinitis pigmentosa. Homozygous HGSNAT variant c.370A>T leads to partial skipping of exon 3. In other patients with retinitis pigmentosa, a complex HGSNAT variant, c.[398G>C; 1843G>A] on one allele, and c.1843G>A on the other allele, is found. HGSNAT activity levels in blood leukocytes of patients are reduced compared with healthy controls, but usually higher than those in mucopolysaccharidosis type IIIC patients. All patients are diagnosed with non-syndromic retinitis pigmentosa and do not exhibit neurological deterioration, or any phenotypic features consistent with in mucopolysaccharidosis type IIIC. Four of the patients are over 60 years old, exceeding by far the life expectancy of mucopolysaccharidosis IIIC patients
medicine
-
overview, design and synthesis of substrate and internal standard conjugates as substrates in enzyme assay for confirmation of enzyme deficiency using a combination of affinity chromatography and electrospray ionization mass spectrometry
medicine
-
mucopolysaccharidosis type IIIC or Sanfilippo syndrome type C is an autosomal recessive disorder caused by deficiency of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klein, U.; Kresse, H.; Von Figura, K.
Sanfilippo syndrome type C: deficiency of acetyl-CoA: alpha-glucosaminide N-acetyltransferase in skin fibroblasts
Proc. Natl. Acad. Sci. USA
75
5185-5189
1978
Homo sapiens
Reynertson, R.; Campbell, P.; Ford, J.D.; Jacobsson, I.; Roden, L.; Thompson, J.N.
New oligosaccharides from heparin and heparan sulfate and their use as substrates for heparin-degrading enzymes
J. Biol. Chem.
258
7449-7459
1983
Homo sapiens
Meikle, P.J.; Whittle, A.M.; Hopwood, J.J.
Human acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Kinetic characterization and mechanistic interpretation
Biochem. J.
308
327-333
1995
Homo sapiens
-
Voznyi, Y.V.; Karpova, E.A.; Dudukina, T.V.; Tsvetkova, I.V.; Boer, A.M.; Janse, H.C.; van Diggelen, O.P.
A fluorometric enzyme assay for the diagnosis of Sanfilippo disease C (MPS III C)
J. Inherit. Metab. Dis.
16
465-472
1993
Homo sapiens
Taute, A.; Watzig, K.; Simons, B.; Lohaus, C.; Meyer, H.E.; Hasilik, A.
Presence of detergent-resistant microdomains in lysosomal membranes
Biochem. Biophys. Res. Commun.
298
5-9
2002
Homo sapiens
Gerber, S.A.; Turecek, F.; Gelb, M.H.
Design and synthesis of substrate and internal standard conjugates for profiling enzyme activity in the Sanfilippo syndrome by affinity chromatography/electrospray ionization mass spectrometry
Bioconjug. Chem.
12
603-615
2001
Homo sapiens
Nelson, K.; Melville, E.L.; Meikle, P.J.; Anson, D.S.
Immortalisation of a mucopolysaccharidosis type IIIC fibroblast cell line via expression of SV40 T antigen
Cell Biol. Int.
27
567-570
2003
Homo sapiens
Hrebicek, M.; Mrazova, L.; Seyrantepe, V.; Durand, S.; Roslin, N.M.; Noskova, L.; Hartmannova, H.; Ivanek, R.; Cizkova, A.; Poupetova, H.; Sikora, J.; Urinovska, J.; Stranecky, V.; Zeman, J.; Lepage, P.; Roquis, D.; Verner, A.; Ausseil, J.; Beesley, C.E.; Maire, I.; Poorthuis, B.J.; van de Kamp, J.
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
Am. J. Hum. Genet.
79
807-819
2006
Homo sapiens (Q68CP4), Homo sapiens, Mus musculus (Q3UDW8), Mus musculus
Ausseil, J.; Landry, K.; Seyrantepe, V.; Trudel, S.; Mazur, A.; Lapointe, F.; Pshezhetsky, A.V.
An acetylated 120-kDa lysosomal transmembrane protein is absent from mucopolysaccharidosis IIIC fibroblasts: a candidate molecule for MPS IIIC
Mol. Genet. Metab.
87
22-31
2006
Homo sapiens (Q68CP4)
Feldhammer, M.; Durand, S.; Mrazova, L.; Boucher, R.M.; Laframboise, R.; Steinfeld, R.; Wraith, J.E.; Michelakakis, H.; van Diggelen, O.P.; Hrebicek, M.; Kmoch, S.; Pshezhetsky, A.V.
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene
Hum. Mutat.
30
918-925
2009
Homo sapiens
Feldhammer, M.; Durand, S.; Pshezhetsky, A.V.
Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C
PLoS ONE
4
e7434
2009
Homo sapiens
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
J. Biol. Chem.
285
31233-31242
2010
Homo sapiens (Q68CP4), Homo sapiens
Haer-Wigman, L.; Newman, H.; Leibu, R.; Bax, N.M.; Baris, H.N.; Rizel, L.; Banin, E.; Massarweh, A.; Roosing, S.; Lefeber, D.J.; Zonneveld-Vrieling, M.N.; Isakov, O.; Shomron, N.; Sharon, D.; Den Hollander, A.I.; Hoyng, C.B.; Cremers, F.P.; Ben-Yosef, T.
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT)
Hum. Mol. Genet.
24
3742-3751
2015
Homo sapiens (Q68CP4), Homo sapiens
Choi, Y.; Tuzikov, A.B.; Ovchinnikova, T.V.; Bovin, N.V.; Pshezhetsky, A.V.
Novel direct assay for acetyl-CoA:alpha-glucosaminide N-acetyltransferase using BODIPY-glucosamine as a substrate
JIMD Rep.
28
11-18
2015
Homo sapiens (Q68CP4), Homo sapiens
Fedele, A.O.; Isenmann, S.; Kamei, M.; Snel, M.F.; Trim, P.J.; Proud, C.G.; Hopwood, J.J.
Lysosomal N-acetyltransferase interacts with ALIX and is detected in extracellular vesicles
Biochim. Biophys. Acta
1865
1451-1464
2018
Homo sapiens (Q68CP4), Homo sapiens
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Transporter Classification Database (TCDB): 9.B.169.4.1
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