2.4.1.255: protein O-GlcNAc transferase
This is an abbreviated version!
For detailed information about protein O-GlcNAc transferase, go to the full flat file.
Word Map on EC 2.4.1.255
Reaction
Synonyms
beta-N-acetylglucosaminidase, EGF domain-specific O-GlcNAc transferase, EGF domain-specific O-linked N-acetylglucosamine transferase, EOGT, EOGT1, epidermal growth factor domain-specific O-GlcNAc transferase, glycosyltransferase OGT, Gtf1, GtfA, hOGT, HsOGT, human OGT, mammalian OGT, mOGT, More, N-acetylglucosamine transferase, N-acetylglucosamine-peptide N-acetylglucosaminyltransferase, N-acetylglucosaminyltransferase, ncOGT, nuclear cytoplasmic OGT, nucleocytoplasmic glycosyltransferase, nucleocytoplasmic OGT, O-GlcNAc protein, O-GlcNAc transferase, O-GlcNAc transferase OGT, O-GlcNAc-transferase, O-GlcNAcase, O-glycosylated protein p135, O-linked beta-N-acetylglucosamine transferase, O-linked beta-N-acetylglucosaminyltransferase, O-linked GlcNAc transferase, O-linked N-acetylglucosamine transferase, O-linked N-acetylglucosaminyltransferase, O-N-acetylglucosamine (O-GlcNAc) transferase, OGT, OGT p110, OGT protein, ogta, OGTase, OGTase protein, ogtb, p135, Protein SECRET AGENT, SEC, SECRET AGENT, sOGT, spindly, SPY, super sex combs, Sxc, Synpcc7942_0051, transferase OGT, UDP-GlcNAc: polypeptide O-N-acetylglucosaminyltransferase, UDP-GlcNAc:polypeptidyl transferase, UDP-N-acetylglucosaminyl transferase, uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase, XcOGT, XcOGT protein
ECTree
2.4.1.255 protein O-GlcNAc transferaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.4.1.255 - protein O-GlcNAc transferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
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
-
donor analogue displacement probes
1-(4-acetamidophenyl)-4-(naphthalen-2-yl)-1H-1,2,3-triazole
i.e. APNT, cell-permeable inhibitor, able to inhibit OGlcNAcylation in cells without significant effects on cell viability
1-(4-acetamidophenyl)-4-([1,1'-biphenyl]-4-yl)-1H-1,2,3-triazole
i.e. APBT, cell-permeable inhibitor, able to inhibit OGlcNAcylation in cells without significant effects on cell viability
1-(4-chloroacetamidophenyl)-4-(diphenylhydroxymethyl)-1H-1,2,3-triazole
-
3-(2-adamantanylethyl)-2-[(4-chlorophenyl)azamethylene]-4-oxo-1,3-thiazaperhydroine-6-carboxylic acid
-
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
-
donor analogue displacement probes
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)
4-methoxyphenyl 5-acetyl-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
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
about 30% inhibition with a 3fold excess of inhibitor
5'-O-(hydroxy[3-[(2R,3R)-3-hydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
-
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-trihydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
-
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-tris(benzyloxy)pyrrolidin-2-yl]propyl]phosphoryl)uridine
-
5'-O-[hydroxy(phosphonomethyl)phosphoryl]uridine
-
non-hydrolysable alpha,beta-methylene bisphosphonate analogue with the diphosphate oxygen replaced by a methylene group
5'-O-[[(2-(N-acetyl-akoga-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-(N-acetyl-beta-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-alpha-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-beta-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-(N-acetyl-alpha-D-glucosaminopyranosyl)propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3R)-3-(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3S,4S)-3,4-bis(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
ethyl (R)-4-(2-(2-((2-ethoxy-2-oxoethyl)(thiophen-2-ylmethyl)amino)-2-oxo-1-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)ethyl)phenoxy)butanoate
-
-
ethyl (R)-N-(2-((7-chloro-2-oxo-1,2-dihydroquinoline)-6-sulfonamido)-2-(2-methoxyphenyl)acetyl)-N-(thiophen-2-ylmethyl)glycinate
-
-
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
methyl (R)-N-(2-(2-methoxyphenyl)-2-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)acetyl)-N-(thiophen-2-ylmethyl)glycinate
-
-
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
UDP-GalNAc
-
UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-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
UDP
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
-
binds weakly
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
-
a sub-millimolar inhibitor of hOGT and substrate binding probe
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
-
binds weakly
UDP-GlcNAc
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UTP
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
additional information
-
testing UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro. These analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation
-
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
-
additional information
-
testing UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro. These analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation
-
