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Information on EC 3.2.1.169 - protein O-GlcNAcase and Organism(s) Mus musculus and UniProt Accession Q9EQQ9

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IUBMB Comments
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
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Mus musculus
UNIPROT: Q9EQQ9
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
o-glcnac hydrolase, o-glcnac-selective n-acetyl-beta-d-glucosaminidase, btgh84, glycoside hydrolase o-glcnacase, cpoga, cytoplasmic o-glcnacase, endos-like endoglycosidase, cpnagj, o-glcnac-selective-n-acetyl-beta-d-glucosaminidase, neutral o-glcnacase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NCOAT
bifunctional nucleo-cytoplasmic protein with both O-GlcNAcase and histone acetyltransferase domains
O-linked N-acetylglucosaminase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
?
fluorescein di(N-acetyl-beta-D-glucosaminide) + H2O
fluorescein mono(N-acetyl-beta-D-glucosaminide) + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O
[protein]-L-serine + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O
[protein]-L-threonine + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O
[protein]-L-serine + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O
[protein]-L-threonine + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HPDP-biotin
treatment with a sulfhydrylspecific biotinylation reagent, HPDP-biotin, to biotinylate any accessible free cysteine residue in the native enzyme. Treatment is able to inhibit enzymatic activity, suggesting that the cysteine residue playing a role in catalysis is modified
N-ethylmaleimide
treatment is able to inhibit enzymatic activity, suggesting that the cysteine residue playing a role in catalysis is modified
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 1.4
4-nitrophenyl N-acetyl-beta-D-glucosaminide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 54.9
4-nitrophenyl N-acetyl-beta-D-glucosaminide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6 - 112
4-nitrophenyl N-acetyl-beta-D-glucosaminide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
D174N mutant displayed a reduced catalytic efficiency at the wild type enzyme's optimal pH as well as in the basic pH range. It exhibits a marked shift in pH optimum to the pH 5-5.5 range
6.5 - 7
optimum for the wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme knockout mice show nearly complete perinatal lethality associated with low circulating glucose and low liver glycogen stores. Enzyme loss leads to defects in metabolic homeostasis culminating in obesity and insulin resistance
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OGA_MOUSE
916
0
103162
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C166S
site-directed mutagenesis
C878S
site-directed mutagenesis, comparable level of O-GlcNAcase activity as wild-type enzyme
D174N
site-directed mutagenesis
D175A
site-directed mutagenesis
D177N
site-directed mutagenesis
DELTA250-345
protein missing amino acids 250-345, due to the removal of exon 8
DELTA250-398
lacks amino acids 250-398 in the protein due to the specific excision of exons 8 and 9
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a pUC118-pTM hybrid expression vector containing the full length and splice variant mouse NCOAT
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toleman, C.; Paterson, A.J.; Kudlow, J.E.
Location and characterization of the O-GlcNAcase active site
Biochim. Biophys. Acta
1760
829-839
2006
Mus musculus (Q9EQQ9)
Manually annotated by BRENDA team
Keembiyehetty, C.; Love, D.C.; Harwood, K.R.; Gavrilova, O.; Comly, M.E.; Hanover, J.A.
Conditional knock-out reveals a requirement for O-linked N-acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis
J. Biol. Chem.
290
7097-7113
2015
Mus musculus (Q9EQQ9), Mus musculus
Manually annotated by BRENDA team