Information on EC 2.4.1.255 - protein O-GlcNAc transferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.255
-
RECOMMENDED NAME
GeneOntology No.
protein O-GlcNAc transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
show the reaction diagram
The N-acetyl-D-glucosaminyl residue is transferred to threonine or serine hydroxy groups on the polypeptide.
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-
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transglycosylation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Other types of O-glycan biosynthesis
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protein O-[N-acetyl]-glucosylation
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-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
no activity in Escherichia coli
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-
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Streptococcus pneumoniae serotype 4
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UniProt
Manually annotated by BRENDA team
Streptococcus pneumoniae serotype 4 ATCC BAA-334
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adhesin PsrP + UDP-GlcNAc
? + UDP
show the reaction diagram
capsid protein of Plum pox virus + UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-[capsid protein of Plum pox virus]
show the reaction diagram
casein kinase II + UDP-GlcNAc
? + UDP
show the reaction diagram
-
-
-
-
?
casein kinase II + UDP-N-azidoacetylglucosamine
? + UDP
show the reaction diagram
-
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
? + UDP
show the reaction diagram
-
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
UDP + ?
show the reaction diagram
-
much poorer substrate than Nup 62
-
-
?
crystalline alpha + UDP-GlcNAc
? + UDP
show the reaction diagram
-
i.e. small heat-shock protein crystalline alpha
-
-
?
GSK-3beta + UDP-GlcNAc
UDP + ?
show the reaction diagram
-
rabbit skeletal muscle glycogen synthase kinase (GSK) -3beta
-
-
?
KENSPCVTPVSTA + UDP-GlcNAc
? + UDP
show the reaction diagram
-
-
-
?
KKKYPGGSTPVSSANMM + UDP-4-deoxy-GalNAc
? + UDP
show the reaction diagram
-
-
-
-
?
KKKYPGGSTPVSSANMM + UDP-4-deoxy-GlcNAc
? + UDP
show the reaction diagram
-
22.2% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-6-deoxy-GalNAc
? + UDP
show the reaction diagram
-
37.7% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-6-deoxy-GlcNAc
? + UDP
show the reaction diagram
-
85% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
? + UDP
show the reaction diagram
-
peptide acceptor derived from casein kinase II
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-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
UDP + ?
show the reaction diagram
-
Pep-CKII, known natural substrate for OGT
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-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAz
? + UDP
show the reaction diagram
-
peptide acceptor derived from casein kinase II
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-
?
KKKYPGGSTPVSSANMM + UDP-GlcNPr
? + UDP
show the reaction diagram
-
the close vicinity between Met501 and the N-acyl group of GlcNPr, as well as the hydrophobic environment near Met501, are responsible for the selective binding of UDP-GlcNPr
-
-
?
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
-
-
?
nucleoporin p62 + UDP-N-azidoacetylglucosamine
? + UDP
show the reaction diagram
-
-
-
-
?
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
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-
?
RBL-2 + UDP-GlcNAc
? + UDP
show the reaction diagram
-
acceptor RBL-2 is a key regulator of entry into cell division. Residue Ser420 is a possible O-GlcNAc site in RBL-2. Substitution of Ser 420 inhibits OGT activity
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?
UDP-GlcNAc + Abi2 protein
UDP + N-acetly-D-glucosaminyl-[Abi2 protein]
show the reaction diagram
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-
-
-
?
UDP-GlcNAc + Abl2 protein
UDP + N-acetly-D-glucosaminyl-[Ab12 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Ablim2 protein
UDP + N-acetly-D-glucosaminyl-[Ablim2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Add1 protein
UDP + N-acetly-D-glucosaminyl-[Add1 protein]
show the reaction diagram
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?
UDP-GlcNAc + AIPVSREEK
UDP + AIPV-(GlcNAc)SREEK
show the reaction diagram
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-
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?
UDP-GlcNAc + Amot protein
UDP + N-acetly-D-glucosaminyl-[Amot protein]
show the reaction diagram
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-
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?
UDP-GlcNAc + Arhgap32 protein
UDP + N-acetly-D-glucosaminyl-[Arhgap32 protein]
show the reaction diagram
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-
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?
UDP-GlcNAc + Atf2 protein
UDP + N-acetly-D-glucosaminyl-[Atf2 protein]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + beta-amyloid associated protein
GlcNAc-beta-amyloid associated protein + UDP
show the reaction diagram
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?
UDP-GlcNAc + c-MYC intron binding protein 1
UDP + N-acetyl-D-gluosaminyl-[c-MYC intron binding protein 1]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + calcium/calmodulin-dependent kinase IV
UDP + N-acetyl-D-glucosaminyl-[calcium/calmodulin-dependent kinase IV]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + CARM1 protein
UDP + N-acetyl-D-glucosaminyl-[CARM1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + CKII peptide
UDP + N-acetyl-D-glucosaminyl-[CKII peptide]
show the reaction diagram
UDP-GlcNAc + CKII peptide
UDP + N-acetylglucosaminyl-CKII alpha-peptide
show the reaction diagram
-
PGGSTPVSSANMM
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?
UDP-GlcNAc + Clasp2 protein
UDP + N-acetly-D-glucosaminyl-[Clasp2 protein]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + Clip1 protein
UDP + N-acetly-D-glucosaminyl-[Clip1 protein]
show the reaction diagram
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?
UDP-GlcNAc + Cnot4 protein
UDP + N-acetly-D-glucosaminyl-[Cnot4 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Cnskr2 protein
UDP + N-acetly-D-glucosaminyl-[Cnskr2 protein]
show the reaction diagram
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-
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?
UDP-GlcNAc + Corp1b protein
UDP + N-acetly-D-glucosaminyl-[Corp1b protein]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + Crtc1 protein
UDP + N-acetly-D-glucosaminyl-[Crtc1 protein]
show the reaction diagram
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-
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?
UDP-GlcNAc + CSNK1D
CSNK1D-GlcNAc + UDP
show the reaction diagram
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
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UDP-GlcNAc + DCTN1
DCTN1-GlcNAc + UDP
show the reaction diagram
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
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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
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?
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 + Dlgap2 protein
UDP + N-acetly-D-glucosaminyl-[Dlgap2 protein]
show the reaction diagram
-
-
-
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?
UDP-GlcNAc + Dvl1 protein
UDP + N-acetly-D-glucosaminyl-[Dv11 protein]
show the reaction diagram
-
-
-
-
?
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 + Enah protein
UDP + N-acetly-D-glucosaminyl-[Enah protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Foxk2 protein
UDP + N-acetly-D-glucosaminyl-[Foxk2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Foxp1 protein
UDP + N-acetly-D-glucosaminyl-[Foxp1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Frs3 protein
UDP + N-acetly-D-glucosaminyl-[Frs3 protein]
show the reaction diagram
-
-
-
-
?
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 + H2O
UPD + GlcNAc
show the reaction diagram
UDP-GlcNAc + host cell factor C1
UDP + N-acetyl-D-gluosaminyl-[host cell factor C1]
show the reaction diagram
-
the enzyme both O-GlcNAcylates the HCF-1N subunit and directly cleaves the host cell factor-1PRO repeat
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-
?
UDP-GlcNAc + ITISETPSSTTTTQITK
UDP + ITI-(GlcNAc)SETPSSTTTTQITK
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + KKFELLPTPPLSPSRR
UDP + KKFELLP-(GlcNAc)TPPLSPSRR
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Mamld1 protein
UDP + N-acetly-D-glucosaminyl-[Mamld1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + MYPT1
MYPT1-GlcNAc + UDP
show the reaction diagram
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
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UDP-GlcNAc + Nav1 protein
UDP + N-acetly-D-glucosaminyl-[Nav1 protein]
show the reaction diagram
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-
-
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?
UDP-GlcNAc + Ncoa1 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Ncoa2 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Ncoa5 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa5 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + NFATc1
O-GlcNAc-NFATc1 + UDP
show the reaction diagram
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-
-
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?
UDP-GlcNAc + Nfia protein
UDP + N-acetly-D-glucosaminyl-[Nfia protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Notch epidermal growth factor 20 repeat
UDP + N-acetyl-D-gluosaminyl-[Notch epidermal growth factor 20 repeat]
show the reaction diagram
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-
-
?
UDP-GlcNAc + Nr3c1 protein
UDP + N-acetly-D-glucosaminyl-[Nr3c1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Nup 62 protein
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosaminyl-[Nup62 protein]
show the reaction diagram
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-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
show the reaction diagram
UDP-GlcNAc + O-GlcNAcase
O-GlcNAcase-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + p62 protein
UDP + N-acetyl-D-glucosaminyl-[p62 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + PGC-1alpha
UDP + N-acetyl-D-gluosaminyl-[PGC-1alpha]
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 + Plec protein
UDP + N-acetly-D-glucosaminyl-[Plec protein]
show the reaction diagram
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-
-
-
?
UDP-GlcNAc + Psd3 protein
UDP + N-acetly-D-glucosaminyl-[Psd3 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Rapgef2 protein
UDP + N-acetly-D-glucosaminyl-[Rapgef2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Rasgrf2 protein
UDP + N-acetly-D-glucosaminyl-[Rasgrf2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + SAP130
SAP130-GlcNAc + UDP
show the reaction diagram
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
-
UDP-GlcNAc + Sirt2 protein
UDP + N-acetly-D-glucosaminyl-[Sirt2 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Ss18l1 protein
UDP + N-acetly-D-glucosaminyl-[Ss1811 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Stat3 protein
UDP + N-acetly-D-glucosaminyl-[Stat3 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Tab1 protein
UDP + N-acetly-D-glucosaminyl-[Tab1 protein]
show the reaction diagram
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-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
show the reaction diagram
UDP-GlcNAc + tau protein
GlcNAc-tau protein + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Tbr1 protein
UDP + N-acetly-D-glucosaminyl-[Tbr1 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Tle4 protein
UDP + N-acetly-D-glucosaminyl-[Tle4 protein]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + Tnik protein
UDP + N-acetly-D-glucosaminyl-[Tnik protein]
show the reaction diagram
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-
-
-
?
UDP-GlcNAc + TRAK1 protein
UDP + N-acetyl-D-glucosaminyl-[TRAK1 protein]
show the reaction diagram
UDP-GlcNAc + transcription factor FoxM1
O-GlcNAc-transcription factor FoxM1 + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + transcription factor NFAT
UDP + N-acetyl-D-glucosaminyl-[transcription factor NFAT]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + transcription factor NFkappaB
UDP + N-acetyl-D-glucosaminyl-[transcription factor NFkappaB]
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + YPGGSTPVSSANMM
UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
show the reaction diagram
UDP-GlcNAc + YSDSPSTST
UDP + GlcNAc-YSDSPSTST
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
YSDSP-(GlcNAc)STST + UDP
show the reaction diagram
-
coupled enzyme assay of C-654
-
-
?
UDP-GlcNAc + YSPTSPSYSPTSPS
UDP + Y-(GlcNAc)SPT-(GlcNAc)SPSYSPT-(GlcNAc)SPS
show the reaction diagram
-
YSPTSPSYSPTSPS is a poor substrate
-
-
?
UDP-GlcNAc + Znf532 protein
UDP + N-acetly-D-glucosaminyl-[Znf532 protein]
show the reaction diagram
-
-
-
-
?
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
-
-
?
UDP-N-acetyl-D-glucosamine + KKKYPGGSTPVSSANMM
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + YPGGSTPVSSANMM
UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
?
show the reaction diagram
-
UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine is a very poor (3200times slower) donor substrate compared to UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine
show the reaction diagram
-
the enzyme transfers N-acetylglucosamine from the sugar donor UDP-GlcNAc onto specific serine or threonine residues of nucleocytoplasmic proteins with inversion of configuration at the anomeric center
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
UDP + [protein]-O3-(N-acetyl-D-glucosaminyl)-L-serine
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-threonine
UDP + [protein]-O3-(N-acetyl-D-glucosaminyl)-L-threonine
show the reaction diagram
-
-
-
-
?
YSDSPSTST + UDP-GlcNAc
UDP + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Ca2+
-
activates
Mn2+
-
activates, highest activity in the presence of 1 mM Mn2+
additional information
-
the enzyme is metal-independent
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2Z)-2-[(4-chlorophenyl)imino]-4-oxo-3-(2-tricyclo[3.3.1.1(3,7)]dec-1-ylethyl)-1,3-thiazinane-6-carboxylic acid
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donor analogue displacement probes
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
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donor analogue displacement probes
3-[2-adamantanylethyl]-2-[[4-chlorophenyl]azamethylene]-4-oxo-1,3-thiazaperhyd roine-6-carboxylic acid
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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)
4-methoxyphenyl 5-acetyl-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
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the compound fully inactivates the enzyme within 5 min at a 1:1 ratio of inhibitor:enzyme
4-methoxyphenyl 6-chloro-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
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about 30% inhibition with a 3fold excess of inhibitor
5'-O-[hydroxy(phosphonomethyl)phosphoryl]uridine
-
non-hydrolysable alpha,beta-methylene bisphosphonate analogue with the diphosphate oxygen replaced by a methylene group
alloxan
ATP
-
has a much lower affinity for OGT
GlcNAc
-
inhibited by GlcNAc, but not by GalNAc
goblin1
bisubstrate-linked inhibitor in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C3 linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates
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N-ethylmaleimide
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O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino N-phenylcarbamate
-
-
phenyl 3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
-
about 70% inhibition with a 3fold excess of inhibitor
phenyl 3-hydroxy-5-methoxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
-
about 10% inhibition with a 3fold excess of inhibitor
phenyl 3-hydroxy-5-nitro-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
-
about 60% inhibition with a 3fold excess of inhibitor
phenyl 6-chloro-2-oxobenzo[d]oxazole-3(2H)-carboxylate
-
donor analogue displacement probes
phenyl 6-chloro-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
-
the compound causes an irreversible loss of enzyme activity, about 48% inhibition with a 3fold excess of inhibitor
thiouridine diphosphate
-
SUDP
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
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
UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine
-
effective inhibitor
UDP-S-GlcNAc
UMP
-
UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
uridine 5'-[[(2-acetylamino-5-hydroxymethyl-benzyl)-phosphono]phosphate]
-
designed to mimic the transition state of the natural donor involved in the enzymatic reaction. The analogue shows low activity as an inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ataxin-10
-
CoCl2
-
stress treatment induces higher levels of OGT protein expression
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
dithiothreitol
-
increases the activity of wild type OGT
ethanol
-
stress treatment induces higher levels of OGT protein expression
H2O2
-
stress treatment induces higher levels of OGT protein expression
hyperglycemia
-
increases O-GlcNAc levels in pancreatic beta cells, which appears to interfere with beta-cell function
-
Insulin
-
tyrosine phosphorylation of OGT increases significantly after a 10 min insulin treatment
-
NaCl
-
stress treatment induces higher levels of OGT protein expression
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of O-GlcNAcase, increase of the level of O-GlcNAc modifications
Sodium arsenite
-
stress treatment induces higher levels of OGT protein expression
UDP-N-acetyl-D-glucosamine
-
-
UVB light
-
stress treatment induces higher levels of OGT protein expression
-
vanadate
-
tyrosine phosphatase inhibitor sodium vanadate, treatment increases OGT activity. When insulin is added to cells preincubated with sodium vanadate, there is a further increase in OGT activity versus inhibitor alone
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
Nup 62 protein
-
-
-
0.000025 - 0.000227
Nup62
-
0.00335
OIP106 protein
-
apparent Km of OGT for the OID of OIP106 protein
-
0.107 - 0.215
PGGSTPVSSANMM
0.3695
UDP-4-deoxy-GalNAc
-
pH 7.4, 37C
0.1418
UDP-6-deoxy-GlcNAc
-
pH 7.4, 37C
0.0005 - 11.8
UDP-GlcNAc
0.2821
UDP-GlcNPr
-
pH 7.4, 37C
-
0.0047 - 0.0085
UDP-N-azidoacetylglucosamine
-
0.16
YSDSPSTST
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000073 - 1.76
UDP-GlcNAc
0.0015 - 0.0085
UDP-N-azidoacetylglucosamine
-
2.48
YSDSPSTST
Homo sapiens
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 1.15
UDP-GlcNAc
276
0.001 - 0.003
UDP-N-azidoacetylglucosamine
210490
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0362
UDP-S-GlcNAc
pH 7.5, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.053
(2Z)-2-[(4-chlorophenyl)imino]-4-oxo-3-(2-tricyclo[3.3.1.1(3,7)]dec-1-ylethyl)-1,3-thiazinane-6-carboxylic acid
0.06
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
Homo sapiens
-
sOGT
0.009
5'-O-[hydroxy(phosphonomethyl)phosphoryl]uridine
Homo sapiens
-
-
0.018
alloxan
Homo sapiens
-
-
0.86
ATP
Rattus norvegicus
-
-
0.008
goblin1
Homo sapiens
O15294
pH 7.5, 22C
-
50
KCl
Rattus norvegicus
-
about
4
NaCl
Rattus norvegicus
-
about
45
NaH2PO4
Rattus norvegicus
-
-
0.01 - 0.027
phenyl 6-chloro-2-oxobenzo[d]oxazole-3(2H)-carboxylate
0.0002 - 0.018
UDP
0.041
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
Homo sapiens
-
-
0.093
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
Homo sapiens
-
-
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
0.0683
UDP-S-GlcNAc
Drosophila melanogaster
Q7KJA9
pH 7.5, temperature not specified in the publication
0.019
UMP
Rattus norvegicus
-
-
0.0002 - 0.0005
UTP
additional information
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
Homo sapiens
-
for ncOGT IC50 value is about 100-150 microM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00111
-
last purification step
0.161
-
-
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
5.5 - 7
-
-
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 30C, almost a complete loss of activity occurs at 37C. At 33C there is a 45% decrease in OGT activity
additional information
-
hOGT assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
stress treatment, different temperatures are representative of different basal levels of thermotolerance
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.63
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
infected with the asexual intraerythrocytic stage of the malaria parasite, Plasmodium falciparum. Comparison of O-glycosylation in Plasmodium falciparum-infected and uninfected erythrocytes
Manually annotated by BRENDA team
-
mammary epithelial cell
Manually annotated by BRENDA team
-
mammary epithelial cell
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
neuro-2a murine neuroblastoma cell, ATCC
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
lowest expression
Manually annotated by BRENDA team
contains very little of the ogt transcripts
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
x * 70000, shortest isoform sOGT, SDS-PAGE
73000
-
theoretical
75000
-
highly purified C-654, truncated mOGT recombinant
103000
114000
-
fusion protein
116000
340000
-
on molecular sieve chromatography
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotrimer
trimer
-
kinetic analyses of the full-length trimer and the truncated monomer forms of OGT
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure of the protein domains I and II, conserved amino acid sequences
-
N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D135), crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc, to 2.7 A resolution. The enzyme adopts the canonical OGT fold with the bilobal arrangement of two Rossmann-like domains, as well as the additional TPR-like helices (535566) in the N-terminal of the catalytic domain. As a result, the TPRs are in close association with the glycosyltransferase domain and the catalytic site is aligned with the channel along the main axis of the TPR superhelix
a binary complex with UDP and a ternary complex with UDP and peptide substrate YPGGSTPVSSANMM, hanging drop vapor diffusion method
-
cocrystallization of identified substrate peptides with OGT, derived from retinoblastoma-like protein 2 (RBL2411-422, KENPAVTPVSTA), proto-oncogene tyrosine protein kinase receptor Ret (Ret660-672, AQAFPVSYSSSGA), keratin-7 (KER77-19, SPVFTSRSAAFSC) and lamin B1 (LAMIN179-191, KLSPSPSSRVTVS). The peptide is tethered into a common binding mode by a combination of van der Waals interactions and hydrogen bonds that restrict torsional freedom in the -3 to +2 subsites only
-
hybrid quantum mechanics/molecular mechanics analysis of reaction paths using alpha-phosphate and Asp554 as the catalytic bases. The mechanism with alpha-phosphate acting as the base is favorable. The reaction has a rate-limiting free energy barrier of 23.5 kcal/mol, whereas reactions utilizing Asp554 and water-assisted alpha-phosphate have barriers of 41.7 and 40.9 kcal/mol, respectively
-
in complex with inhibitor goblin1, to 3.15 A resolution. UDP adopts the same conformation as observed in the OGT Michaelis complex and the peptide occupies the -4 to +2 subsites with a similar backbone conformation. The three-carbon linker connects the two components without introducing any strain, allowing both the UDP moiety and the peptide part of the inhibitor to adopt the optimal position in the binding site, mimicking the natural substrates
three-dimensional structure of the protein domains I and II, conserved amino acid sequences
-
vapour diffusion crystallisation experiments are performed
-
X-ray crystallography
-
three-dimensional structure of the protein domains I and II, conserved amino acid sequences
-
in complex with UDP and GlcNAc. GtfA reveals a beta-meander add-on domain beyond the catalytic domain, which is distinct from the all-alpha-tetratricopeptide repeats in the two structure-known OGTs. This add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein
Streptococcus pneumoniae serotype 4
X-ray crystallography
-
vapour diffusion crystallisation experiments are performed
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purified enzyme is stable and can be stored for several months at -20C with negligible loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, at pH 6.0-6.5
-
gel filtration
-
HisTrap nickel column chromatography
-
immunopurified
-
Ni2+-affinity chromatography
-
nickel affinity chromatography and gel filtration
-
nickel affinity chromatography, purified p110 subunit
-
recombinant enzyme
-
two-step purification, isolation of a relatively pure complex that contains both OGT and serine/threonine phosphatases
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of more than 50 of human cDNA clones and other ESTs suggest that the mammalian ogt gene encodes several splice variants
-
baculovirus expression
-
cloning and expression of OGT in insect cells
-
expressed in Escherichia coli
expressed in Escherichia coli and expressed in HeLa cells
expressed in Escherichia coli and HEK-293 cells
-
expressed in Escherichia coli Tuner cells
-
expressed in Escherichia coli; expressed in Escherichia coli
expressed in HEK-293T cells
-
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
expression in Escherichia coli, N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D1352)
expression in HeLa cells
-
full length and functional human mOGT is difficult to be expressed in Escherichia coli, truncated mOGT recombinant (C-654) is constructed and expressed
-
modified with both O-GlcNAc and tyrosine phosphorylation when overexpressed in insect cells
-
ncOGT, mOGT, and sOGT constructs are cloned into a modified pET-24b vector for expression as C-terminal His8 fusions. Expression in Escherichia coli
-
overexpressed FLAGtagged human OGT in VSM cells
-
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
-
purified recombinant 110 kDa subunit of OGTase expressed in Escherichia coli
-
recombinant expression in Escherichia coli
-
recombinant production of human sOGT and ncOGT in Escherichia coli
-
SEC protein expressed in Escherichia coli
the mitochondrial version of human OGT is subcloned into the pSos vector in-frame with the human Sos protein
-
using the insect cell baculovirus system to overexpress p110 subunit
-
when co-expressed in Escherichia coli SEC modifies PPV-CP
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sec spy double mutant
double-mutant embryos aborted at various stages of development and no double-mutant seedlings are obtained. These results indicate that OGT activity is required during gametogenesis and embryogenesis with lethality occurring when parentally derived SEC, SPY, and/or O-GlcNAcylated proteins become limiting
sec-1
has a tDNA insertion within the exon encoding the ninth tetratricopeptide repeat, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
sec-2
contains an insertion within an intron adjacent to exons encoding the putative catalytic portion of the protein, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
spy-3
Columbia (Col-0) background, has a Gly-to-Ser substitution in the C-terminal region of the protein. The spy plants have defects in a number of processes, including gibberellin and cytokinin responses, flowering, circadian regulation, and light inhibition of hypocotyls elongation
H537A
5.6% of wild-type activity
H596F
3.0% of wild-type activity
K872M
mutation of a key catalytic lysine, crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc. Inactive
C835A
-
the mutation has no effect compared with wild type enzyme
C836S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
C839S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
C911A
-
active site mutant
D407A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D422A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, produces a 50-100% increase in activity
D431A
-
single-point mutation, peptide-binding mutant
D438A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D488A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D505A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D549A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D554A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D925N
-
single-point mutation, UDP-GlcNAc-binding mutant
DELTAN-DELTAKEN-FoxM1
-
O-GlcNAcation required the N terminus
E482A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E556A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E568A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F439A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F460A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F721A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
F752A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 110% activity compared to wild type
F776A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
G402S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G453S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G472A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G538S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
H498A
-
single-point mutation, peptide-binding mutant
H558A
-
active site mutant
H558D
-
active site mutant
H558E
-
active site mutant
H901Y
-
active site mutant
H920A
-
active site mutant, deleterious
hOGT (26-end)
-
mutant
K842M
-
single-point mutation, UDP-GlcNAc-binding mutant
L796A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
N458A
-
single-point mutation, peptide-binding mutant
ncOGT
-
long OGT isoform, nucleocytoplasmic OGT, microinjected into immature oocytes prior to progesterone incubation
Q839A
-
single-point mutation, UDP-GlcNAc-binding mutant
Q839E
-
active site mutant
Q839N
-
active site mutant, low specific activity
R637A
-
single-point mutation, peptide-binding mutant
sOGT
-
N-terminally truncated isoform, short OGT, microinjected into immature oocytes prior to progesterone incubation
T560A
-
single-point mutation, UDP-GlcNAc-binding mutant
T914A
-
active site mutant
T922A
-
active site mutant
W536A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
W735A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W748A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W812A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W878A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
Y387A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, mutation is not included for enzymatic analysis, because not sufficient amounts of protein could be produced
Y434A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
Y539A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
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
G350D
mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain
H280A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
K445A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine