Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.169 - protein O-GlcNAcase and Organism(s) Clostridium perfringens and UniProt Accession Q0TR53

for references in articles please use BRENDA:EC3.2.1.169
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Clostridium perfringens
UNIPROT: Q0TR53
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Clostridium perfringens
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
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 beta-D-N-acetylglucosaminide + H2O
4-methylumbelliferone + beta-D-N-acetylglucosamine
show the reaction diagram
-
-
-
?
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
fluorogenic substrate, 4MU-NAG
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-beta-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
-
-
-
?
3,4,6-triacetyl-O-GlcNAc-Fmoc-Ser-OH + H2O
?
show the reaction diagram
-
-
-
-
?
3,4,6-triacetyl-O-GlcNAc-Fmoc-Thr-OH + H2O
?
show the reaction diagram
-
-
-
-
?
[dHCF peptide]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O
[dHCF peptide]-L-threonine + N-acetyl-D-glucosamine
show the reaction diagram
-
i.e. VPSgTMSAN
-
-
?
[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
-
-
-
-
?
[TAB1 protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O
[TAB1 protein]-L-serine + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
-
-
-
?
[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
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-(trifluoromethyl)-2,3-dihydro-1H-1,4-diazepine
-
Ala-Cys(S-GlcNAc)-Ala
pseudosubstrate
GlcNAcstatin C
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
PUGNAc, transition state mimic
streptozotocin
STZ, diabetogenic compound, acts as a suicide inhibitor
GlcNAcstatin B
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029 - 0.041
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
0.0029 - 0.1
4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
0.121
4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013 - 11
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
10.5 - 65
4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
0.2
4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0683 - 3620
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.146
5-(trifluoromethyl)-2,3-dihydro-1H-1,4-diazepine
pH and temperature not specified in the publication
0.000066
GlcNAcstatin B
pH and temperature not specified in the publication
0.0000046 - 0.0000981
GlcNAcstatin C
0.0000163
GlcNAcstatin G
pH and temperature not specified in the publication
0.0000054
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
-
0.000037
thiamet G
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
Ala-Cys(S-GlcNAc)-Ala
Clostridium perfringens
-
0.0000145
GlcNAcstatin B
Clostridium perfringens
pH and temperature not specified in the publication
0.0000429
GlcNAcstatin G
Clostridium perfringens
pH and temperature not specified in the publication
0.0000086 - 0.000024
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
0.064
streptozotocin
Clostridium perfringens
-
0.0000626
thiamet G
Clostridium perfringens
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
significant sequence homology to the human O-GlcNAcase N-terminus
sitting drop vapor diffusion method, using 0.175 M CdSO4 and 0.1 M sodium acetate at pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D297N
rather inactive mutant
D298N
rather inactive mutant
D401A
rather inactive mutant
N390A
as active as wild-type
N396A
rather inactive mutant
V331C
mutation of Val331 to cysteine results in a mutant enzyme with unaltered steady-state kinetics compared with wild-type CpOGA
W490A
Y335F
rather inactive mutant
D298N
-
inactive
D401A
-
the mutation abrogates the interactions with the N-acetyl-D-glucosamine O4 and O6 hydroxyl groups23
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione affinity chromatography
IMAC Sepharose column chromatography, Hi-Trap QFF column chromatography, and Superdex 200 gel filtration
glutathione Sepharose column chromatography and Superdex S200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and overexpressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)-Gold cells
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme is a drug target for the treatment of Alzheimer's and cardiovascular disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dorfmueller, H.C.; Borodkin, V.S.; Schimpl, M.; van Aalten, D.M.F.
GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation
Biochem. J.
420
221-227
2009
Clostridium perfringens (Q0TR53), Homo sapiens
Manually annotated by BRENDA team
Rao, F.V.; Dorfmueller, H.C.; Villa, F.; Allwood, M.; Eggleston, I.M.; van Aalten, D.M.
Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
EMBO J.
25
1569-1578
2006
Clostridium perfringens (Q0TR53)
Manually annotated by BRENDA team
Borodkin, V.S.; Rafie, K.; Selvan, N.; Aristotelous, T.; Navratilova, I.; Ferenbach, A.T.; van Aalten, D.M.F.
O-GlcNAcase fragment discovery with fluorescence polarimetry
ACS Chem. Biol.
13
1353-1360
2018
Clostridium perfringens (Q0TR53), Clostridium perfringens, Homo sapiens (O60502), Homo sapiens
Manually annotated by BRENDA team
Mariappa, D.; Selvan, N.; Borodkin, V.; Alonso, J.; Ferenbach, A.T.; Shepherd, C.; Navratilova, I.H.; van Aalten, D.M.F.
A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development
Biochem. J.
470
255-262
2015
Clostridium perfringens
Manually annotated by BRENDA team