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Information on EC 3.2.1.169 - protein O-GlcNAcase and Organism(s) Bacteroides thetaiotaomicron and UniProt Accession Q89ZI2

for references in articles please use BRENDA:EC3.2.1.169
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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.
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This record set is specific for:
Bacteroides thetaiotaomicron
UNIPROT: Q89ZI2
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Bacteroides thetaiotaomicron
Synonyms
beta-N-acetylglucosaminidase, BtGH84, CP40, CpNagJ, CpOGA, cytoplasmic O-GlcNAcase, endo-beta-N-acetylglucosaminidase, EndoS-like endoglycosidase, glycoside hydrolase O-GlcNAcase, hexosaminidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BtGH84
O-GlcNAc hydrolase
291171
-
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
2-acetamido-2-deoxy-5-fluoro-beta-D-glucopyranosyl fluoride + H2O
fluoride + N-acetyl-beta-D-glucosaminide
show the reaction diagram
-
a substrate contains a modest leaving group as well as a poor nucleophile, the catalytic efficiency of the enzyme is synergistically impaired. Testing a wide range of such substrates and obtained co-crystals of BtGH84, to test if under the right conditions, such a substrate might be trapped in the active site unhydrolyzed
-
-
?
3,4-difluorophenyl 2-deoxy-2-difluoroacetamido-beta-D-glucopyranoside + H2O
3,4-difluorophenol + 2-deoxy-2-difluoroacetamido-beta-D-glucopyranose
show the reaction diagram
-
a substrate contains a modest leaving group as well as a poor nucleophile, the catalytic efficiency of the enzyme is synergistically impaired. Testing a wide range of such substrates and obtained co-crystals of BtGH84, to test if under the right conditions, such a substrate might be trapped in the active site unhydrolyzed
-
-
?
4-methylumbelliferyl 2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-glucopyranose
show the reaction diagram
-
substrate with a 4-methylumbelliferone leaving group. A substrate contains a modest leaving group as well as a poor nucleophile, the catalytic efficiency of the enzyme is synergistically impaired. Testing a wide range of such substrates and obtained co-crystals of BtGH84, to test if under the right conditions, such a substrate might be trapped in the active site unhydrolyzed
-
-
?
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl N-difluoroacetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-difluoroacetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl N-fluoroacetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-fluoroacetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl N-trifluoroacetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-trifluoroacetyl-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
4-nitrophenyl N-acetyl-beta-D-thioglucosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-thioglucosamine
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
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
NAG-thiazoline
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
-
PUGNAc
streptozotocin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 1
4-methylumbelliferyl 2-acetamido-2-deoxy-beta-D-glucopyranoside
0.016 - 36
4-nitrophenyl N-acetyl-beta-D-glucosaminide
1.4
4-nitrophenyl N-acetyl-beta-D-thioglucosaminide
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
bell-shaped pH-activity profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
visualization of the reaction coordinate of O-GlcNAc hydrolases
-
X-ray crystal structure of BtGH84 in complex with the inhibitor NAG-thiazoline. Hanging drop vapor diffusion method
-
X-ray crystallography
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D242A
-
site-directed mutant, 2800fold lower catalytic efficiency than wild-type
D242N
D243A
-
site-directed mutant, 110fold lower catalytic efficiency than wild-type
D243N
N372A
-
site-directed mutant
Y137F
-
site-directed mutant
Y282F
-
site-directed mutant
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
affinity chromatography using nickel-affinity chromatography followed by gel filtration
-
the N-terminal His6-tagged recombinant BtGH84 protein is purified
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
soluble BtGH84 is expressed in the cytoplasm of Escherichia coli
-
the N-terminal His6-tagged recombinant BtGH84 protein is expressed
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
He, Y.; Martinez-Fleites, C.; Bubb, A.; Gloster, T.M.; Davies, G.J.
Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase
Carbohydr. Res.
344
627-631
2009
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron (Q89ZI2)
Manually annotated by BRENDA team
He, Y.; Macauley, M.S.; Stubbs, K.A.; Vocadlo, D.J.; Davies, G.J.
Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase
J. Am. Chem. Soc.
132
1807-1809
2010
Bacteroides thetaiotaomicron (Q89ZI2)
Manually annotated by BRENDA team
Dennis, R.J.; Taylor, E.J.; Macauley, M.S.; Stubbs, K.A.; Turkenburg, J.P.; Hart, S.J.; Black, G.N.; Vocadlo, D.J.; Davies, G.J.
Structure and mechanism of a bacterial beta -glucosaminidase having O-GlcNAcase activity
Nat. Struct. Mol. Biol.
13
365-371
2006
Bacteroides thetaiotaomicron (Q89ZI2)
Manually annotated by BRENDA team
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