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Information on EC 2.4.1.255 - protein O-GlcNAc transferase and Organism(s) Rattus norvegicus and UniProt Accession P56558

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.255 protein O-GlcNAc transferase
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:
Rattus norvegicus
UNIPROT: P56558
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Rattus norvegicus
Synonyms
beta-N-acetylglucosaminidase, EGF domain-specific O-GlcNAc transferase, EGF domain-specific O-linked N-acetylglucosamine transferase, EOGT, EOGT1, glycosyltransferase OGT, Gtf1, GtfA, hOGT, HsOGT, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylglucosamine-peptide N-acetylglucosaminyltransferase
248
-
O-GlcNAc transferase
O-GlcNAc-transferase
O-glycosylated protein p135
248
-
O-linked beta-N-acetylglucosamine transferase
265215
-
O-linked beta-N-acetylglucosaminyltransferase
248
-
O-linked GlcNAc transferase
248
-
O-linked N-acetylglucosamine transferase
OGT p110
265215
-
OGT protein
265215
-
OGTase
OGTase protein
248
-
UDP-GlcNAc: polypeptide O-N-acetylglucosaminyltransferase
265215
-
UDP-N-acetylglucosaminyl transferase
248
-
uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
248
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:protein-O-beta-N-acetyl-D-glucosaminyl transferase
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
UDP-GlcNAc + CKII peptide
UDP + N-acetylglucosaminyl-CKII alpha-peptide
show the reaction diagram
-
PGGSTPVSSANMM
-
-
?
UDP-GlcNAc + dynamin-related protein 1
UDP + dynamin-related protein 1-GlcNAc
show the reaction diagram
-
dynamin-related protein 1 is O-linked-N-acetyl-glucosamine-glycosylated at threonine 585 and 586
-
-
?
UDP-GlcNAc + p62 protein
UDP + N-acetyl-D-glucosaminyl-[p62 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + GlcNAc-YSDSPSTST
show the reaction diagram
-
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
? + UDP
show the reaction diagram
-
-
-
-
?
mitochondrial motor-adaptor protein milton + UDP-GlcNAc
? + UDP
show the reaction diagram
-
-
mitochondrial motor-adaptor protein Milton is a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues
-
?
nucleoporin p62 + UDP-GlcNAc
? + UDP
show the reaction diagram
-
high affinity substrate
-
-
?
OIP106 protein + UDP-GlcNAc
O-GlcNAc-OIP106 protein + UDP
show the reaction diagram
-
N-terminal deletions of OIP106 are generated as S-tagged constructs: DELTAnCC, DELTA491, DELTA639, DELTA859
-
-
?
UDP-GlcNAc + AIPVSREEK
UDP + AIPV-(GlcNAc)SREEK
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + beta-amyloid associated protein
GlcNAc-beta-amyloid associated protein + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + DELTA639 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA639 protein]
show the reaction diagram
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + DELTAnCC protein
UDP + N-acetyl-D-glucosaminyl-[DELTAnCC protein]
show the reaction diagram
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + ITISETPSSTTTTQITK
UDP + ITI-(GlcNAc)SETPSSTTTTQITK
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + KKFELLPTPPLSPSRR
UDP + KKFELLP-(GlcNAc)TPPLSPSRR
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + PGGSTPVS(PO3)-SANMM
? + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + PGGSTPVSSANMM
UDP + PGGSTPV-(GlcNAc)SSANMM
show the reaction diagram
-
PGGSTPVSSANMM is the best acceptor
-
-
?
UDP-GlcNAc + tau protein
GlcNAc-tau protein + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
show the reaction diagram
UDP-GlcNAc + YSPTSPSYSPTSPS
UDP + Y-(GlcNAc)SPT-(GlcNAc)SPSYSPT-(GlcNAc)SPS
show the reaction diagram
-
YSPTSPSYSPTSPS is a poor substrate
-
-
?
UDP-GlcNAc + [YSPTSPSYSPTSPS]5
UDP + [Y-(GlcNAc)SP-(GlcNAc)TSPSYSP-(GlcNAc)TSPS]5
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc DELTA491 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA491 protein]
show the reaction diagram
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
manganese choride 5 mM, essential for binding, although divalent cations are not required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[2-adamantanylethyl]-2-[[4-chlorophenyl]azamethylene]-4-oxo-1,3-thiazaperhyd roine-6-carboxylic acid
-
endothelin 1 effects are not observed when vessels are previously instilled with anti-O-GlcNAc transferase antibody or after incubation with an O-GlcNAc transferase inhibitor (100 microMol)
ATP
-
has a much lower affinity for OGT
thiouridine diphosphate
-
SUDP
UDP
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UDP-galactose
-
much lower affinity for OGT compared with UDP-GlcNAc
UDP-GalNAc
-
; UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
UDP-GlcNAc
UDP-glucose
-
much lower affinity for OGT compared with UDP-GlcNAc
UMP
-
UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
additional information
-
the isolated tetratricopeptide repeat domain of OGT competitively inhibits glycosylation of the OID protein, but does not inhibit glycosylation of small peptides, providing kinetic evidence for the role of the tetratricopeptide repeat domain as a protein substrate docking site
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ataxin-10
-
Atx-10 increases OGT activity 2fold
-
D-glucose
-
immunoblot analysis of OGTase expression in RASM cells. The amount of the 78 kDa subunit is significantly increased in the high glucose, but no significant increase in the amount of the 110 kDa subunit is observed. OGTase expression and activity increased in the RASM cells cultured in the 20 mM glucose
additional information
-
nearly all of the peptides became better acceptors as the concentration of UDP-GlcNAc increased with the exception of the YSPTSPSYSPTSPS
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00335
OIP106 protein
-
apparent Km of OGT for the OID of OIP106 protein
-
0.107 - 0.215
PGGSTPVSSANMM
0.000545 - 0.217
UDP-GlcNAc
additional information
additional information
-
kinetic studies suggest that OGT functions through a random bi-bi kinetic mechanism and that the protein has three distinct binding constants for the UDPGlcNAc sugar donor
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86
ATP
Rattus norvegicus
-
-
50
KCl
Rattus norvegicus
-
about
4
NaCl
Rattus norvegicus
-
about
45
NaH2PO4
Rattus norvegicus
-
-
0.0002 - 0.018
UDP
0.013
UDP-galactose
Rattus norvegicus
-
much lower affinity for OGT compared with UDP-GlcNAc
0.016
UDP-GalNAc
Rattus norvegicus
-
-
0.00018 - 0.00025
UDP-GlcNAc
0.0042
UDP-glucose
Rattus norvegicus
-
much lower affinity for OGT compared with UDP-GlcNAc
0.019
UMP
Rattus norvegicus
-
-
0.0002 - 0.0005
UTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00111
-
last purification step
additional information
-
activity of OGT on acceptor substrates is dependent on UDP-GlcNAc concentrations. The observation that OGT has three separate binding constants for UDP-GlcNAc suggested that UDP-GlcNAc concentration could directly affect OGT activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
activity remaining fairly high up to pH 7.5 while dropping rapidly below 6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
24 - 27
-
a slight loss in enzyme activity is seen at 30°C, almost a complete loss of activity occurs at 37°C. At 33°C there is a 45% decrease in OGT activity
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
distribution of OGTase in the aorta is examined by immunofluorescence microscopy
Manually annotated by BRENDA team
additional information
-
no activity in kidney
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
unlike previously described glycosyltransferases, OGT is localized to the cytosol and nucleus
Manually annotated by BRENDA team
additional information
immunoelectron microscopy shows that OGT is localized to the euchromatin of the nucleus and around the secretory granules of exocrine acinar cells and endocrine islet cells
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
increased extracellular glucose decreases mitochondrial motility in hippocampal axons, and OGT overexpression reduces axonal mitochondrial motility and density. The mitochondrial motor-adaptor protein Milton is a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
OGT1_RAT
1036
0
115606
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
x * 70000, shortest isoform sOGT, SDS-PAGE
78000
103000
-
x * 103000, mitochondrial isoform mOGT, SDS-PAGE
110000
116000
-
x * 116000, nucleocytoplasmic isoform ncOGT, SDS-PAGE
78000
110000
340000
-
on molecular sieve chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotrimer
-
2 * 110000 + 1 * 78000, SDS-PAGE
heterodimer
-
1 * 110000 + 1 * 78000
heterotrimer
-
2 * 110000, 1 * 78000 (alpha2beta)
trimer
-
kinetic analyses of the full-length trimer and the truncated monomer forms of OGT
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA2.5OGT
-
Baculovirus-produced recombinant, is partially active toward the OID protein substrate, but is fully active toward the CKII peptide substrate
DELTA5.5OGT
-
Baculovirus-produced recombinant
full-length OGT
-
Baculovirus-produced recombinant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
cytosolic OGT activity is stable at 24°C but was rapidly inactivated at 37°C (t1/2 = 20 min). Nuclear OGT is not inactivated at 37°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purified enzyme is stable and can be stored for several months at -20°C with negligible loss of activity
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, at pH 6.0-6.5
-
immunopurified
-
nickel affinity chromatography, purified p110 subunit
-
two-step purification, isolation of a relatively pure complex that contains both OGT and serine/threonine phosphatases
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
overexpression of the Ogt gene encoding the 110 kDa alpha-subunit in Escherichia coli and transiently in HEK293 cells, DNA sequence analysis: gene Ogt is no member of a multigene family, the sequence contains multiple tandem repeats of the tetratricopeptide repeat motif
-
baculovirus expression
-
purified recombinant 110 kDa subunit of OGTase expressed in Escherichia coli
-
using the insect cell baculovirus system to overexpress p110 subunit
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform ncOGT level decreases gradually after 1 month and reduces by up to 60% when rats are 2 years old. The brain sOGT level is nearly undetectable during early development and increases markedly after 15 days after birth, although its level decreases again at age of 2 years
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haltiwanger, R.S.; Blomberg, M.A.; Hart, G.W.
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
J. Biol. Chem.
267
9005-9013
1992
Rattus norvegicus
Manually annotated by BRENDA team
Kreppel, L.K.; Blomberg, M.A.; Hart, G.W.
Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
J. Biol. Chem.
272
9308-9315
1997
Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Konrad, R.J.; Tolar, J.F.; Hale, J.E.; Knierman, M.D.; Becker, G.W.; Kudlow, J.E.
Purification of the O-glycosylated protein p135 and identification as O-GlcNAc transferase
Biochem. Biophys. Res. Commun.
288
1136-1140
2001
Rattus norvegicus
Manually annotated by BRENDA team
Akimoto, Y.; Comer, F.I.; Cole, R.N.; Kudo, A.; Kawakami, H.; Hirano, H.; Hart, G.W.
Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
Brain Res.
966
194-205
2003
Rattus norvegicus
Manually annotated by BRENDA team
Wells, L.; Kreppel, L.K.; Comer, F.I.; Wadzinski, B.E.; Hart, G.W.
O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
J. Biol. Chem.
279
38466-38470
2004
Rattus norvegicus
Manually annotated by BRENDA team
Maerz, P.; Stetefeld, J.; Bendfeldt, K.; Nitsch, C.; Reinstein, J.; Shoeman, R.L.; Dimitriades-Schmutz, B.; Schwager, M.; Leiser, D.; Ozcan, S.; Otten, U.; Ozbek, S.
Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain
J. Biol. Chem.
281
20263-20270
2006
Homo sapiens (O15294), Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Hyperglycemia and the O-GlcNAc transferase in rat aortic smooth muscle cells: elevated expression and altered patterns of O-GlcNAcylation
Arch. Biochem. Biophys.
389
166-175
2001
Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Hanover, J.A.; Yu, S.; Lubas, W.B.; Shin, S.H.; Ragano-Caracciola, M.; Kochran, J.; Love, D.C.
Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
Arch. Biochem. Biophys.
409
287-297
2003
Homo sapiens, Mus musculus, Mus musculus (Q8CGY8), Rattus norvegicus
Manually annotated by BRENDA team
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Localization of the O-linked N-acetylglucosamine transferase in rat pancreas
Diabetes
48
2407-2413
1999
Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Lima, V.V.; Giachini, F.R.; Carneiro, F.S.; Carneiro, Z.N.; Saleh, M.A.; Pollock, D.M.; Fortes, Z.B.; Carvalho, M.H.; Ergul, A.; Webb, R.C.; Tostes, R.C.
O-GlcNAcylation contributes to augmented vascular reactivity induced by endothelin 1
Hypertension
55
180-188
2010
Rattus norvegicus
Manually annotated by BRENDA team
Kreppel, L.K.; Hart, G.W.
Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
J. Biol. Chem.
274
32015-32022
1999
Rattus norvegicus
Manually annotated by BRENDA team
Iyer, S.P.; Hart, G.W.
Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
J. Biol. Chem.
278
24608-24616
2003
Rattus norvegicus
Manually annotated by BRENDA team
Cheung, W.D.; Sakabe, K.; Housley, M.P.; Dias, W.B.; Hart, G.W.
O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
J. Biol. Chem.
283
33935-33941
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Okuyama, R.; Marshall, S.
UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme
J. Neurochem.
86
1271-1280
2003
Rattus norvegicus
Manually annotated by BRENDA team
Gawlowski, T.; Suarez, J.; Scott, B.; Torres-Gonzalez, M.; Wang, H.; Schwappacher, R.; Han, X.; Yates, J.R.; Hoshijima, M.; Dillmann, W.
Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes
J. Biol. Chem.
287
30024-30034
2012
Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Liu, Y.; Li, X.; Yu, Y.; Shi, J.; Liang, Z.; Run, X.; Li, Y.; Dai, C.L.; Grundke-Iqbal, I.; Iqbal, K.; Liu, F.; Gong, C.X.
Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
PLoS ONE
7
e43724
2012
Rattus norvegicus (P56558)
Manually annotated by BRENDA team
Pekkurnaz, G.; Trinidad, J.C.; Wang, X.; Kong, D.; Schwarz, T.L.
Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
Cell
158
54-68
2014
Rattus norvegicus
Manually annotated by BRENDA team
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