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

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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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Bacteroides thetaiotaomicron
UNIPROT: Q89ZI2
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Word Map
The taxonomic range for the selected organisms is: Bacteroides thetaiotaomicron
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, o-glcnac-selective-n-acetyl-beta-d-glucosaminidase, neutral o-glcnacase, cpnagj, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BtGH84
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
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 (Q89ZI2), Bacteroides thetaiotaomicron
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