Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase and Organism(s) Homo sapiens and UniProt Accession P21980

for references in articles please use BRENDA:EC2.3.2.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.13 protein-glutamine gamma-glutamyltransferase
IUBMB Comments
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P21980
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transglutaminase, factor xiii, tissue transglutaminase, tgase, factor xiiia, transglutaminase 2, microbial transglutaminase, mtgase, tgase 2, protein 4.2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tissue transglutaminase
-
tissue transglutaminase 2
-
tissue-TG
-
transglutaminase
-
type 2 transglutaminase
-
factor XIII
-
-
factor XIIIa
fibrin stabilizing factor
-
-
-
-
fibrinoligase
-
-
-
-
glutaminylpeptide gamma-glutamyltransferase
-
-
-
-
glutamyltransferase, glutaminylpeptide gamma-
-
-
-
-
hTG2
-
-
Laki-Lorand factor
-
-
microbial transglutaminase
-
-
polyamine transglutaminase
-
-
-
-
protein 4.2
-
R-glutaminyl-peptide:amine gamma-glutamyl transferase
-
-
-
-
TG-2
-
-
TGase
TGase 2
-
-
Tgase 3
TGase-2
-
-
TGase2
-
-
tissue transglutaminase
tissue transglutaminase 2
-
-
transglutaminase
transglutaminase 1
-
transglutaminase 3
-
transglutaminase 6
-
transglutaminase factor XIII
-
-
transglutaminase type II
-
-
transglutaminase-2
-
-
transglutaminase2
-
-
tTG-2
-
-
type I transglutaminase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-glutamine:amine gamma-glutamyltransferase
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
CAS REGISTRY NUMBER
COMMENTARY hide
80146-85-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-APE(gamma-Cad-2,4-dinitrophenyl)QEA + Gly-OMe
?
show the reaction diagram
-
-
-
?
5-(biotinamido)pentylamine + N,N-dimethylated casein
? + NH3
show the reaction diagram
-
-
-
?
Ac-PNPQLPF-OH + alkylamine
?
show the reaction diagram
-
-
-
?
Ac-PQLPF-NH2 + putrescine
?
show the reaction diagram
-
-
-
?
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
alpha2 plasmin inhibitor + ?
?
show the reaction diagram
-
-
-
?
ApoE glutamine + alkylamine
ApoE N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
show the reaction diagram
dimethyl casein glutamine + putrescine
?
show the reaction diagram
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
show the reaction diagram
gliadin glutamine + alkylamine
gliadin N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
N,N'-dimethyl casein glutamine + biotinylated pentylamine
?
show the reaction diagram
the enzymatic activity is determined by measuring the fluorescence of biotinylated pentylamine crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
show the reaction diagram
the enzymatic activity of TG2 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
show the reaction diagram
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
show the reaction diagram
-
-
-
?
N-Cbz-Glu(gamma-4-nitrophenylester)Gly + alkylamine
4-nitrophenol + ?
show the reaction diagram
-
-
-
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
show the reaction diagram
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
?
transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
Z-Gln-Gly + putrescine
?
show the reaction diagram
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
show the reaction diagram
10-kDa heat shock protein-bound gamma-glutamine + methylamine
10-kDa heat shock protein N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + Abeta1-40
?
show the reaction diagram
-
residues 1-40 of beta-amyloid protein
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + N-methyl-casein
?
show the reaction diagram
-
-
-
-
?
60-kDa heat shock protein-bound gamma-glutamine + methylamine
60-kDa heat shock protein N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
actin-bound gamma-glutamine + methylamine
actin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
alpha-actin-bound gamma-glutamine + methylamine
alpha-actin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
alpha-N-t-butyloxycarbonyl-L-Lys-CH2-CH2-dansyl + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
alphaB-crystallin + ?
?
show the reaction diagram
-
-
formation of water-insoluble dimers or polymers
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val
?
show the reaction diagram
-
i.e. beta-amyloid protein peptide comprising residues 1-40
-
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + N,N-dimethylated casein
?
show the reaction diagram
-
transpeptidation
-
-
?
benzyloxycarbonyl-Pro-Gln-Nle-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casein + glycine ethylester
?
show the reaction diagram
-
-
-
-
?
betaB2-crystallin + ?
?
show the reaction diagram
-
-
formation of water-insoluble dimers or polymers
-
?
biotinyl-5-pentylamine + N,N'-dimethylcasein
?
show the reaction diagram
-
covalent incorporation of biotinyl-5-pentylamine into N,N'-dimethylcasein
-
-
?
biotinylated TVQQEL + calcium binding protein S100A7
?
show the reaction diagram
-
transglutaminase 2
-
-
?
Cbz-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
Cbz-Gln-Gly + alkylamine
Cbz-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
Cbz-L-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
clathrin heavy chain-bound gamma-glutamine + methylamine
clathrin heavy chain N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
show the reaction diagram
cornifin-A is SPR1
-
-
?
cytoskeletal 1 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 1 keratin type II N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
cytoskeletal 2 epidermal keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 2 epidermal keratin type II N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
cytoskeletal 5 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 5 keratin type II N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
cytoskeletal 6A keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 6A keratin type II N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
DQMMLPWPAVAL + spermine
?
show the reaction diagram
-
specific substrate of factor XIII
-
-
?
epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
exendin 4 + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
modification at residues K12 and K27 of exendin 4
-
?
fibronectin-bound gamma-glutamine + 5-biotinamidopentylamine
fibronectin N5-biotinamidopentylglutamine + NH3
show the reaction diagram
-
-
-
-
?
filamin A-bound gamma-glutamine + methylamine
filamin A N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
galectin-3-bound gamma-glutamine + methylamine
galectin-3 N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
H2A histone type 1-bound gamma-glutamine + methylamine
H2A histone type 1 N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
H2B histone type 1-bound gamma-glutamine + methylamine
H2B histone type 1 N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
H4 histone -bound gamma-glutamine + methylamine
H4 histone N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
hornein glutamine + pentylamine
hornein N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
HQSYVDPWMLDH + spermine
?
show the reaction diagram
-
specific substrate of factor XIII
-
-
?
involucrin + N,N'-dimethyl-casein
?
show the reaction diagram
-
-
-
-
?
involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
LGPQSKVIG + glycine-ethylester
?
show the reaction diagram
-
i.e. K9, an optimized sequence based on beta-casein
-
-
?
LGPQSLVIG + glycine ethylester
?
show the reaction diagram
-
i.e. K9(K7L), a modified optimized sequence based on beta-casein
-
-
?
loricrin + N,N'-dimethyl-casein
?
show the reaction diagram
-
-
-
-
?
loricrin + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
monodansyl- cadaverine + actin
?
show the reaction diagram
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
show the reaction diagram
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
show the reaction diagram
-
trivial name dansylcadaverine
-
-
?
N-methyl-casein + dansylcadaverine
?
show the reaction diagram
-
-
-
-
?
N-methyl-casein + O-methyl-Gly
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
neuropeptide Y + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
modification at residue Q34 of neuropeptide Y
-
?
NNEQVSPLTLLKLGN + glycine ethylester
?
show the reaction diagram
-
i.e. alpha2-antiplasmin peptide with modification Q2N
-
-
?
NQENVSPLTLLKLGN + glycine ethylester
?
show the reaction diagram
-
i.e. alpha2-antiplasmin peptide with modification Q4N
-
-
?
NQENVSPLTLLLLGN + glycine ethylester
?
show the reaction diagram
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12L
-
-
?
NQENVSPLTLLRLGN + glycine ethylester
?
show the reaction diagram
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12R
-
-
?
NQEQVSPLTLLKLGN + glycine ethylester
?
show the reaction diagram
-
i.e. alpha2-antiplasmin peptide
-
-
?
nucleophosmin-bound gamma-glutamine + methylamine
nucleophosmin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
orexin B + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
modification at residues Q8 and Q12 of orexin B
-
?
plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
PQPQLPYPQPQLPY-NH2 + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
putrescine + casein
?
show the reaction diagram
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
QLQPFPQPQLPY + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
-
-
?
small proline-rich protein 3 + N,N'-dimethyl-casein
?
show the reaction diagram
-
-
-
-
?
small proline-rich protein 3 + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
spectrin alpha-bound gamma-glutamine + methylamine
spectrin alpha N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
spermidine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
SPR2D glutamine + pentylamine
SPR2D N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
vimentin + 5-(biotinamido)pentylamine
?
show the reaction diagram
-
transglutaminase 5
-
-
?
vimentin + ?
?
show the reaction diagram
-
-
formation of water-insoluble dimers or polymers
-
?
vimentin-bound gamma-glutamine + methylamine
vimentin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
YENHKLPSSWPF + alkylamine
Y-N5-alkylglutaminyl-NHKLPSSWPF + NH3
show the reaction diagram
N-terminally biotinylated peptide substrate
-
-
?
YEQHKLPSSWPF + pentylamine
Y-N5-pentylglutaminyl-QHKLPSSWPF + NH3
show the reaction diagram
N-terminally biotinylated peptide substrate
-
-
?
Z-Gln-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gln-Gly + O-methyl-Gly
?
show the reaction diagram
-
-
-
-
?
[protein]-gamma-glutamine + 5-(biotinamido) pentylamine
?
show the reaction diagram
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
ApoE glutamine + alkylamine
ApoE N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
show the reaction diagram
beta-crystallin, a major structural protein of the eye lens, is an archetypal TG2 substrate. Its target Gln residue is localized to a peptide sequence denoted A25 (TVQQEL), and is crosslinked to a Lys residue near the C-terminus of the same protein
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
show the reaction diagram
the 220 kDa fibronectin monomer harbors multiple Gln residues susceptible to TG2 modification, including sites within its N-terminal collagen/fibrinbinding domain, its central (RGD-containing) integrin-binding domain, and its C-terminal glycosaminoglycan-binding domain. In addition, its N-terminal domain also harbors a high-affinity non-covalent docking site for TG2
-
-
?
gliadin glutamine + alkylamine
gliadin N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
show the reaction diagram
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
show the reaction diagram
-
-
-
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
show the reaction diagram
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
show the reaction diagram
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
Cbz-Gln-Gly + alkylamine
Cbz-Glu-Gly + NH3
show the reaction diagram
-
-
-
-
?
Cbz-L-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
show the reaction diagram
cornifin-A is SPR1
-
-
?
desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
hornein glutamine + pentylamine
hornein N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
SPR2D glutamine + pentylamine
SPR2D N5-pentylglutamine + NH3
show the reaction diagram
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ERp57
TG2 cofactors TRX and ERp57 reversibly regulate TG2 in a redox-dependent manner, and act as on and off switches for the active enzyme
-
thioredoxin
TRX, TG2 cofactors TRX and ERp57 reversibly regulate TG2 in a redox-dependent manner, and act as on and off switches for the active enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
La3+
-
requirement, 0.01-0.1 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
-
1-(6-methylpyridin-2-yl)piperazine
-
1-(6-nitropyridin-3-yl)piperazine
-
1-acetyl-L-prolyl-6-imino-5-oxo-L-norleucyl-L-leucyl-L-prolyl-L-phenylalaninamide
-
1-ethyl-3-(4-methoxyphenyl)-6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
-
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
-
3-iodo-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(3-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid benzyl ester
-
4-(4-acryloylamino-2-chlorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-fluorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-methoxybenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-methylbenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-trifluoromethylbenzenesulfonyl)-piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylamino-3-fluorobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-chlorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-methylbenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-trifluoromethylbenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 3,5-difluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid cyclopentyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid methyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-1-ylmethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-2-ylmethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 2,3-difluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 4-fluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid ethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)[1,4]diazepane-1-carboxylicacid benzyl ester
-
4-(4-acryloylaminobenzenesulfonylamino)piperidine-1-carboxylic acid benzyl ester
-
4-(4-but-2-enoylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-cyanobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-fluoro-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
4-fluoro-N-[(2S)-1-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
4-[(4-acryloylaminobenzenesulfonylamino)methyl]-piperidine-1-carboxylic acid benzyl ester
-
4-[4-(1-oxobut-2-ynylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-cyanoacetylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-ethoxycarbonylvinyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(2-fluoroacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-methylacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-methylbut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-oxopropionylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-(E)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-(Z)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-cyanomethylureido)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-diazo-2-oxopropyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(3-ethoxycarbonylallyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(4,4,4-trifluoro-3-methylbut-2-enoylamino)-benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(4,4,4-trifluorobut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(4-diazo-3-oxobutyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(acryloylmethyl-amino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(ethoxycarbonylmethylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-acryloylamino-3-(isobutylmethylamino)-benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
5-(4-acryloylaminobenzenesulfonyl)-2,5-diazabicyclo-[2.2.1]heptane-2-carboxylic acid tert-butyl ester
-
5-(4-acryloylaminobenzenesulfonyl)hexahydropyrrolo[3,4-c]pyrrole-2-carboxylic acid benzyl ester
-
5-biotinamido pentylamine
5BP, 5BP is widely used in chromogenic TG2 assays, based on the ability of streptavidin conjugates to recognize its biotin substituent with high specificity
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxamide
-
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylic acid
-
6-diazo-5-oxo-L-norleucine
DON
Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
high-affinity irreversible inhibitor of TG2. The inhibitor stabilizes TG2 in an extended conformation that is dramatically different from earlier transglutaminase structures. The active site is exposed, revealing that catalysis takes place in a tunnel, bridged by two tryptophan residues that separate acyl-donor from acyl-acceptor and stabilize the tetrahedral reaction intermediates
acetonitrile
48% residual activity at 5% (v/v)
acrylonitrile
68 and 48% residual activity at 2.5 and 5.0 mM, respectively
CP30a
reversible inhibitor
CP4d
reversible inhibitor
DMF
90% residual activity at 2.5 and 5% (v/v)
EDTA
complete inhibition at 10 mM
ethenesulfonic acid (4-bromophenyl)amide
-
GTP
the protein transamidase activity of TG2 is positively regulated by calcium and negatively regulated by GTP
KCC009
a specific tTG inhibitor
LDN-27219
-
methyl 5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylate
-
monodansyl cadaverine
MDC
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
-
N-(2-bromophenyl)acrylamide
-
N-(3-bromophenyl)acrylamide
-
N-(4-bromobenzyl)acrylamide
-
N-(4-bromophenyl)acrylamide
-
N-(4-bromophenyl)propionamide
-
N-(4-fluorophenyl)acrylamide
-
N-(4-[4-[2-(2-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-(4-[4-[2-(3-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]- phenyl)acrylamide
-
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-phenylacrylamide
-
N-[(5S)-5-(2-cyclohexylacetamido)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(3-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-bromophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-chlorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-iodophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-methylphenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamothioyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamoyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)methyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-(4-phenylpiperazin-1-yl)hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-4-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-[6-(trifluoromethyl)pyridin-3-yl]piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]-5-(2,2,2-trifluoroacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(3-methylphenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-fluorobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrophenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridine-2-carbonyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-fluoropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamothioyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylmethanesulfonyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(pyridin-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-3-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[(4-fluorophenyl)methyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[4-(4-cyclopentanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
N-[4-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
N-[4-(4-phenylpiperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(4-pyridin-2-ylpiperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(aminomethyl)benzyl]-3-(5-[[[[(E)-2-phenylethenyl]sulfonyl](pyridin-2-ylmethyl)amino]methyl]-1,2,4-oxadiazol-3-yl)benzamide
-
N-[4-(piperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(pyrrolidine-1-sulfonyl)phenyl]acrylamide
-
N-[4-methanesulfonylphenyl]acrylamide
-
N-[4-methoxyphenyl]acrylamide
-
N-[4-nitrophenyl]acrylamide
-
N-[4-phenoxyphenyl]acrylamide
-
N-[4-toluyl]acrylamide
-
N-[4-trifluoromethylphenyl]acrylamide
-
N-[4-[4-(2-phenylcyclopropanecarbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(2-trifluoromethylphenyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(3-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-phenylpropionyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-phenylpropyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-trifluoromethylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(4,4-difluoropiperidine-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(4-phenylbutyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(6-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(6-trifluoromethylpyridin-3-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(octahydroisoquinoline-2-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(octahydroquinoline-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(piperidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(pyrrolidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[5-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-pyridin-2-yl]acrylamide
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyridin-2-yl]acrylamide
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyrimidin-2-yl]acrylamide
-
N-{[(5S)-3-bromo-4,5-dihydro-1,2-oxazol-5-yl]methyl}-5-fluoro-Nalpha-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
NC-I052
irreversible inhibitor
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
-
tert-butyl 4-(4-fluorobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(4-nitrobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(6-chloropyridine-2-carbonyl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-iodopyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-nitropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-phenylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-tert-butylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(pyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-[(4-fluorophenyl)methyl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(methoxycarbonyl)pyridin-3-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(trifluoromethyl)pyridin-3-yl]piperazine-1-carboxylate
-
tert-butyl N6-acryloyl-N2-[(benzyloxy)carbonyl]-L-lysylglycinate
-
ZED1227
an irreversible peptidomimetic TG2-selective inhibitor
[(5R,8S)-8-{[(benzyloxy)carbonyl]amino}-5-(methoxycarbonyl)-2,7-dioxo-9-phenylnonyl](dimethyl)sulfonium bromide
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-ylmethyl]-carbamic acid benzyl ester
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-yl]-carbamic acid benzyl ester
-
[2-[(4-acryloylaminobenzenesulfonyl)methylamino]ethyl]-methylcarbamic acid benzyl ester
-
[4-(4-acryloylpiperazine-1-sulfonyl)phenyl]carbamic acid benzyl ester
-
[4-[(4-aminophenyl)sulfonyl]piperazin-1-yl](cyclopropyl)methanone
-
(1Z)-2-{[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl}ethanehydrazonic acid
-
-
(2-tert-butoxy-2-oxoethyl)(dimethyl)sulfonium
-
-
(2-[[(1R)-3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-1-carboxy-3-oxopropyl]amino]-2-oxoethyl)(dimethyl)sulfanium bromide
-
-
(2-[[4-(methoxycarbonyl)benzyl]oxy]-2-oxoethyl)(dimethyl)sulfonium
-
-
(2-[[6-(methoxycarbonyl)naphthalen-2-yl]methoxy]-2-oxoethyl)(dimethyl)sulfonium
-
-
(2S)-2-[[(benzyloxy)carbonyl]amino]-4-[(prop-2-enoyl)amino]butanoic acid
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(2-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(nicotinamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(prop-2-yn-1-yloxy)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(pyrazine-2-carboxamido)-pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-fluoropyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-methoxypyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-phenylpyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-(benzyloxy)-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-amino-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-benzamido-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-benzyl-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(2-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-chlorophenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-chlorophenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(5-fluoro-1H-indol-3-yl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-fluoropyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-phenylpyrrolidine-1-carboxylate
-
-
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-(2-oxopropylidene)-6-(trifluoromethoxy)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(3-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(4-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(5-bromopyridin-3-yl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-(2-methylpropyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-(cyclohexylmethyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(2-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(3-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(3-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(4-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(4-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(6-methoxypyridin-3-yl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-2-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(2-phenylethyl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(3-phenylpropyl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(propan-2-yl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-phenyl-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-4-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-nitro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(4R)-1-[(benzyloxy)carbonyl]-4-hydroxy-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
-
-
(naphthalen-2-yl)methyl 4-[N-(bromoacetyl)glycyl]piperazine-1-carboxylate
-
-
(R)-quinolin-3-ylmethyl 3-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(1-methyl-1H-benzo[d]imidazol-2-yl)methyl 2-((((S)-3-bromo-4,5-dihydro-isoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(1H-benzo[d]imidazol-2-yl)methyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(R)-1-(naphthalen-2-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(R)-1-(quinolin-3-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(S)-1-(naphthalen-2-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-2,3-dimethoxybenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-3-(benzyloxy)benzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-3-fluorobenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-4-ethynylbenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-benzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-N-(((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)pyrrolidine-2-carboxamide
-
-
(S)-prop-2-yn-1-yl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-2-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-4-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-4-phenyl-2,5-dihydro-1H-pyrrole-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-2-methylpyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)azetidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)piperidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-(2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)amino)-2-oxoethyl)pyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 3-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-3,4-dihydro-1H-pyrido[3,4-b]indole-2(9H)-carboxylate
-
-
(S)-quinolin-4-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-quinoxalin-2-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-tert-butyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)pyrrolidine-1-carboxylate
-
-
1,1'-methanediylbis(1H-indole-2,3-dione)
-
-
1,1'-[(2,5-dimethylbenzene-1,4-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
-
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
-
1,3-dimethyl-2-[(2-oxopropyl)thio]-1H-imidazol-3-ium
-
-
1,3-dimethyl-2-[(2-oxopropyl)thio]imidazolium
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
1-(((3R,5S)-5-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-1-((quinolin-3-ylmethoxy)carbonyl)pyrrolidin-3-yl)-carbamoyl)cyclobutanecarboxylic acid
-
-
1-(ethenylsulfonyl)tricyclo[3.3.1.13,7]decane
-
-
1-(tricyclo[3.3.1.13,7]dec-1-yl)prop-2-en-1-one
-
-
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
2,3-dibromonaphthoquinone
-
0.015 mM, 41.5% inhibition
2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl prop-2-enoate
-
-
2-([2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl]sulfanyl)-1,3,4,5-tetramethyl-1H-imidazol-3-ium bromide
-
-
2-([3-(2-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0015 mM, standard format
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
2-([3-(2-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00082 mM, standard format, at 0.00047 mM, full progress curve
2-([3-(3-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0018 mM, standard format
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00045 mM, full progress curve
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
2-([3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(2-hydroxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00025 mM, full progress curve
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(3-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0014 mM, standard format
2-([3-(3-fluorophenyl)-5-methyl-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0002 mM, full progress curve
2-([3-(3-fluorophenyl)-5-phenyl-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00093 mM, standard format, at 0.00071 mM, full progress curve
2-([3-(3-fluorophenyl)-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00053 mM, full progress curve
2-([3-(3-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0021 mM, standard format
2-([3-(4-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0005 mM, standard format, at 0.00016 mM, full progress curve
2-([3-(4-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0018 mM, standard format
2-([5-(4-fluorophenyl)-4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00029 mM, full progress curve
2-aminonaphthoquinone
-
0.015 mM, 33.4% inhibition
2-bromo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
-
-
2-bromo-3-hydroxynaphthoquinone
-
0.015 mM, 35.4% inhibition
2-chloro-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
-
-
2-[(2-hydrazinoethyl)thio]-3,5-diphenylthieno[2,3-d]pyrimidin-4(3H)-one
-
i.e. LDN-27219, reversible, slow-binding inhibitor that binds at the enzyme’s GTP site or a site that regulates binding of GTP
2-[(3-amino-2-oxopropyl)thio]-3-(3-fluorophenyl)-5-phenylthieno[2,3-d]pyrimidin-4(3H)-one
-
50% inhibition at 0.0053 mM, standard format
2-[(3-benzyl-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0012 mM, standard format, at 0.00048 mM, full progress curve
2-[(3-methyl-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0023 mM, standard format
2-[(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]-N,N-dimethylacetamide
-
-
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)amino]acetohydrazide
-
50% inhibition at 0.0037 mM, full progress curve
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)oxy]acetohydrazide
-
50% inhibition at 0.0045 mM, standard format
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00025 mM, full progress curve
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
-
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
-
2-[(4-oxo-5-phenyl-3-pyridin-3-yl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.002 mM, standard format
2-[(6-methyl-4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0015 mM, standard format, at 0.00016 mM, full progress curve
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
-
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
3-[(6-methyl-4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]propanohydrazide
-
50% inhibition at 0.0013 mM, standard format
5,5'-methanediylbis(1H-indole-2,3-dione)
-
-
5,5'-oxybis(1H-indole-2,3-dione)
-
-
5-(biotinamido)pentylamine
-
-
5-hydroxynaphthoquinone
-
0.015 mM, 46.1% inhibition
6,6'-oxybis(1H-indole-2,3-dione)
-
-
ADP
-
complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
-
benzyl 4-[3-(acryloylamino)-2-oxopropanoyl]piperazine-1-carboxylate
-
-
benzyl 4-[3-[(ethenylsulfonyl)amino]-2-oxopropanoyl]piperazine-1-carboxylate
-
-
benzyl [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
irreversible
benzyl [(2S)-1-(4-acetylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-(4-benzoylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-(morpholin-4-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(phenylacetyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(phenylmethanesulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(propane-2-sulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-2-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-3-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-4-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(thiophene-2-sulfonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(2-aminoethyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(3-aminopropyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(4-aminobutyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(2-chlorophenyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(7-hydroxy-2-oxo-2H-1-benzopyran-3-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
i.e. VA5
benzyl [(2S)-1-[4-(benzenesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(cyclohexanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(ethanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(methanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-1-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-1-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-2-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-2-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-5-[(prop-2-enoyl)amino]pentan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(9S)-19-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-3,10-dioxo-14,17-dioxa-4,11-diazanonadec-1-en-9-yl]carbamate
-
-
BOC-DON-QIV-OMe
-
0.1 mM and 1 mM for normal skin and keloid scar, respectively
Ce3+
-
not reversible by Ca2+
chlorpromazine
-
reverses calmodulin enzyme stimulation
CTP
-
3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
Cu2+
-
-
cystamine
cystamine dihydrochloride
-
1 mM and 10 mM for normal skin and keloid scar, respectively
cysteamine
-
50% inhibition at 0.178 mM
diethyl dicarbonate
-
not without Ca2+
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]sulfonium
-
-
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-ylmethoxy)ethyl]sulfonium
-
-
dimethyl[2-oxo-2-[2-(tricyclo[3.3.1.13,7]dec-1-yl)ethoxy]ethyl]sulfonium
-
-
ERW1041E
-
i.e. (S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
ERW1069
-
i.e. ((S)-1-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)amino)-3-(5-fluoro-1H-indol-3-yl)-1-oxopropan-2-yl)carbamate
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
-
-
Gd3+
-
not reversible by Ca2+
glucosamine
-
the TGase 2 inhibitor, might be an attractive novel target for treatment of malignant cancers
GMP
-
at low levels of Ca2
GSSG
-
reversible inactivation, activity can be restored by treatment with dithiothreitol
GTP-gamma-S
-
inhibition of GTP-hydrolysis
indirubin
-
-
iodoacetamide
isatin
-
weak, reversible inhibitor
isoindigotin
-
-
KCC009
La3+
-
not reversible by Ca2+
LDN-27219
-
reversible, slow-binding inhibitor that appears not to bind at the enzyme’s active site but rather at the enzyme’s GTP site, or a site that regulates binding of GTP. The potency and kinetics of inhibition are dependent on substrate structure and suggest a novel mechanism of inhibition that involves differential binding of LDN-27219 to multiple conformational states of this enzyme
menadione
-
0.015 mM, 97% inhibition
methyl 3-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
-
-
methyl 4-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
-
-
methyl 4-[(acryloyloxy)methyl]benzoate
-
-
methyl 4-[[(bromoacetyl)oxy]methyl]benzoate
-
-
methyl 6-[(acryloyloxy)methyl]naphthalene-2-carboxylate
-
-
methyl 6-[[(bromoacetyl)oxy]methyl]naphthalene-2-carboxylate
-
-
methyl 6-[[(chloroacetyl)oxy]methyl]naphthalene-2-carboxylate
-
-
methyl ketone
-
-
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
-
-
methyl N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycinate
-
-
Monodansylcadaverine
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
-
-
N-(2-aminoethyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)prop-2-enamide
-
-
N-(3-aminopropyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(4-aminobutyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(phenylcarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-acetyl-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
-
active-site inhibitor
N-benzyloxycarbonyl-L-glutaminyl-6-(dimethylsulfonio)-5-oxo-L-norleucine
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
N-ethylmaleimide
-
strong inactivation in the presence of Ca2+, not inhibited in the absence of Ca2+
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]tryptophanamide
-
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(2-phenylethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(naphthalen-2-yloxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-3-ylmethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-4-ylmethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-5-hydroxy-L-tryptophanamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[5-(dimethylamino)naphthalen-2-yl]sulfonyl]-L-tyrosinamide
-
study on pharmacokinetics, pharmacodynamics, and bioavailability
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-3-[(prop-2-enoyl)amino]-L-alanine
-
-
N-[(benzyloxy)carbonyl]-L-alanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-alpha-aspartyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-isoleucyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-5-oxo-6-[(1,3,4,5-tetramethyl-1H-imidazol-3-ium-2-yl)sulfanyl]-L-norleucine
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(diethylsulfonio)-5-oxo-L-norleucine
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-tryptophyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]glycyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N2-[(benzyloxy)carbonyl]-N5-prop-2-enoyl-L-ornithine
-
-
N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycine
-
-
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysinamide
-
-
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysine
-
-
Na-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluorotryptophanamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
-
naphthoquinone
-
0.015 mM, complete inhibition
putrescine
quinolin-3-ylmethyl [(1S)-2-([[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]amino)-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
quinolin-3-ylmethyl [(1S)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
R283
-
specific inhibitor, i.e. 1,3-dimethyl-2-[(2-oxopropyl)thio]imidazolium chloride, complete inhibition at 0.25 mM
S-nitroso-N-acetylpenicillamine
-
NO-donor, 8-16 mM, almost complete inhibition of transglutaminases 1 and 3, weak inhibition of transglutaminase 3
spermidine
-
-
spermine
-
-
Tb3+
-
noncompetitive inhibition of factor XIIIa, at high Ca2+-levels, not reversed by Ca2+
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
-
tricyclo[3.3.1.13,7]dec-1-ylmethyl bromoacetate
-
-
tricyclo[3.3.1.13,7]dec-1-ylmethyl prop-2-enoate
-
-
VA4
-
the inhibitor also inhibits epidermal cancer stem cell invasion with an EC50 of 0.0039 mM
vitamin K1
-
0.015 mM, 10% inhibition
vitamin K2
-
0.015 mM, 75% inhibition
[2-[(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)amino]-2-oxoethyl](dimethyl)sulfanium
-
-
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](diethyl)sulfanium bromide
-
-
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](dimethyl)sulfanium bromide
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
GTP/GDP and Ca2+ are able to compete with one another to convert tTG from the closed- to open-state, and vice versa
GTP
GTP/GDP and Ca2+ are able to compete with one another to convert tTG from the closed- to open-state, and vice versa
thioredoxin-1
thioredoxin-1 is released by macrophages exposed to inflammatory stimuli in sufficient quantity to reduce the tTG C370-C371 disulfide bond, activating the enzyme
Calmodulin/Ca2+
-
0.01-0.2 mM, 3fold activation, inhibition above 0.3 mM, kinetics
-
Chaotropic salts
-
strong activation of epidermal transglutaminase in the presence of Ca2+
-
dithiothreitol
-
3.8fold increase in activity at 10 mM
glutathione
-
reduced, 2.7fold increase in activity at 5 mM
papain
-
limited proteolysis of plasma factor XIII
-
reptilase
-
limited proteolysis of plasma factor XIII
-
thrombin
-
Trypsin
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
Ac-PNPQLPF-OH
at pH 7.0 and 25°C
1.9
alpha2 plasmin inhibitor
at pH 7.5 and 37°C
-
0.0176
N,N'-dimethyl casein glutamine
pH 7.5, 37°C, recombinant TG2 without DNAJA1
-
0.011
N-acetyl-PNPQLPF
apparent value, 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C
0.014
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C
0.007
actin
-
platelet transglutaminase
0.0409
beta-casein
-
-
-
0.011
casein
-
platelet transglutaminase
5.9
CBz-Gln-Gly
-
at pH 7.2 and 37°C
0.0037
involucrin
-
recombinant transglutaminase 5
1.43
LGPQSKVIG
-
37°C, pH 7.4
0.782
LGPQSLVIG
-
37°C, pH 7.4
0.0044
loricrin
-
recombinant transglutaminase 5
-
0.061
methylamine
-
factor XIIIa
11.2 - 30
Nalpha-benzyloxycarbonyl-L-Gln-Gly
1.28
NQENVSPLTLLKLGN
-
37°C, pH 7.4
0.208
NQENVSPLTLLRLGN
-
37°C, pH 7.4
0.459
NQEQVSPLTLLKLGN
-
37°C, pH 7.4
0.6
putrescine
-
-
0.0077
small proline-rich protein 3
-
recombinant transglutaminase 5
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
N,N'-dimethyl casein glutamine
pH 7.5, 37°C, recombinant TG2 without DNAJA1
-
16.1
beta-casein
-
-
-
0.088
CBz-Gln-Gly
-
at pH 7.2 and 37°C
0.00233
involucrin
-
recombinant transglutaminase 5
78
LGPQSKVIG
-
37°C, pH 7.4
44
LGPQSLVIG
-
37°C, pH 7.4
0.0035
loricrin
-
recombinant transglutaminase 5
-
1.86
methylamine
-
factor XIIIa
0.17 - 0.19
Nalpha-benzyloxycarbonyl-L-Gln-Gly
147
NQENVSPLTLLKLGN
-
37°C, pH 7.4
2.8 - 77.3
NQENVSPLTLLRLGN
175
NQEQVSPLTLLKLGN
-
37°C, pH 7.4
0.00433
small proline-rich protein 3
-
recombinant transglutaminase 5
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
85.2
N,N'-dimethyl casein glutamine
pH 7.5, 37°C, recombinant TG2 without DNAJA1
-
0.00083 - 0.017
Nalpha-benzyloxycarbonyl-L-Gln-Gly
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006
Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
-
0.004
CP30a
0.001
CP4d
0.019
NC-I052
0.00041
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.012
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0004
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.004
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0007
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0033
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.003
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0009
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0053
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0054
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.01
1,1'-methanediylbis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.011
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.00016 - 0.045
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.0071 - 0.11
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.00018 - 0.041
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.0015
2-([3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.00014 - 0.019
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.00061 - 0.21
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.006 - 0.5
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
0.00025 - 0.039
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
0.00016 - 0.045
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0071 - 0.22
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.00017 - 0.01
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
0.00018 - 0.041
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0015 - 0.18
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
0.00014 - 0.019
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0011 - 0.19
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
0.00061 - 0.21
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
0.015
5,5'-methanediylbis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.003
5,5'-oxybis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.0011 - 0.09
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
0.11
benzyl [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
pH 9.0, 37°C
0.0521
benzyl [(2S)-1-(4-acetylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0366
benzyl [(2S)-1-(4-benzoylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.02
benzyl [(2S)-1-oxo-1-[4-(phenylacetyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0147
benzyl [(2S)-1-oxo-1-[4-(phenylmethanesulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0091
benzyl [(2S)-1-oxo-1-[4-(propane-2-sulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0401
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(thiophene-2-sulfonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0235
benzyl [(2S)-1-[(2-aminoethyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0305
benzyl [(2S)-1-[(3-aminopropyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0271
benzyl [(2S)-1-[(4-aminobutyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0088
benzyl [(2S)-1-[4-(benzenesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.011
benzyl [(2S)-1-[4-(cyclohexanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.036
benzyl [(2S)-1-[4-(ethanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0064
benzyl [(2S)-1-[4-(methanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0089
benzyl [(2S)-1-[4-(naphthalene-1-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0104
benzyl [(2S)-1-[4-(naphthalene-1-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0134
benzyl [(2S)-1-[4-(naphthalene-2-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0067
benzyl [(2S)-1-[4-(naphthalene-2-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0477
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-5-[(prop-2-enoyl)amino]pentan-2-yl]carbamate
-
pH 6.5, 25°C
0.0129
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0339
benzyl [(9S)-19-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-3,10-dioxo-14,17-dioxa-4,11-diazanonadec-1-en-9-yl]carbamate
-
pH 6.5, 25°C
0.041
isoindigotin
-
pH and temperature not specified in the publication
0.01
methyl ketone
-
pH and temperature not specified in the publication
0.04
methyl N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycinate
-
pH 6.5, 25°C
0.004
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
0.018
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]tryptophanamide
-
-
0.061
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(2-phenylethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.043
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(naphthalen-2-yloxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.078
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-3-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.081
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-4-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.079
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-5-hydroxy-L-tryptophanamide
-
pH 9.0, 37°C
0.087
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.11
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[5-(dimethylamino)naphthalen-2-yl]sulfonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.0013
N-[[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
0.0481
N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycine
-
pH 6.5, 25°C
0.0351
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysinamide
-
pH 6.5, 25°C
0.0603
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysine
-
pH 6.5, 25°C
0.019
Na-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluorotryptophanamide
-
-
0.42
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
0.03
quinolin-3-ylmethyl [(1S)-2-([[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]amino)-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
0.041
quinolin-3-ylmethyl [(1S)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
0.071
Tb3+
-
-
0.0011 - 0.2
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000025
1-ethyl-3-(4-methoxyphenyl)-6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0005 - 0.00058
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
0.000096 - 0.00052
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
0.000069
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000026
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00035
4-(3-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylamino-2-chlorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00019
4-(4-acryloylamino-2-fluorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0025
4-(4-acryloylamino-2-methoxybenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00091
4-(4-acryloylamino-2-methylbenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
4-(4-acryloylamino-2-trifluoromethylbenzenesulfonyl)-piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.013
4-(4-acryloylamino-3-fluorobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000094
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-chlorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00007
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-methylbenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-trifluoromethylbenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00007
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 3,5-difluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00012
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000044
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid cyclopentyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid methyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0000821
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-1-ylmethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00022
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-2-ylmethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0012
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000046
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 2,3-difluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000054
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 4-fluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000072
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid ethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00046
4-(4-acryloylaminobenzenesulfonyl)[1,4]diazepane-1-carboxylicacid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00045
4-(4-acryloylaminobenzenesulfonylamino)piperidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0028
4-(4-but-2-enoylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-(4-cyanobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000078
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000097
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00038
4-[(4-acryloylaminobenzenesulfonylamino)methyl]-piperidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0014
4-[4-(1-oxobut-2-ynylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-cyanoacetylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-ethoxycarbonylvinyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0023
4-[4-(2-fluoroacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-methylacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-methylbut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-oxopropionylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0068
4-[4-(3-(E)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00014
4-[4-(3-(Z)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(3-cyanomethylureido)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.016
4-[4-(3-diazo-2-oxopropyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.091
4-[4-(3-ethoxycarbonylallyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.01
4-[4-(4,4,4-trifluoro-3-methylbut-2-enoylamino)-benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.01 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.01
4-[4-(4,4,4-trifluorobut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.01 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.004
4-[4-(4-diazo-3-oxobutyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0045
4-[4-(acryloylmethyl-amino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.028 - 0.08
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
0.08
4-[4-(ethoxycarbonylmethylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.076
4-[4-acryloylamino-3-(isobutylmethylamino)-benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0003
5-(4-acryloylaminobenzenesulfonyl)-2,5-diazabicyclo-[2.2.1]heptane-2-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00014
5-(4-acryloylaminobenzenesulfonyl)hexahydropyrrolo[3,4-c]pyrrole-2-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.016
ethenesulfonic acid (4-bromophenyl)amide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
N-(2-bromophenyl)acrylamide
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.003
N-(3-bromophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.043
N-(4-bromobenzyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0033
N-(4-bromophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
N-(4-bromophenyl)propionamide
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.029
N-(4-fluorophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00013
N-(4-[4-[2-(2-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000054
N-(4-[4-[2-(3-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00006
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.043
N-phenylacrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0002
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00034
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00009
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00022
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00018
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00011
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00014
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00031
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.0001
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00017
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00039
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.000032
N-[4-(4-cyclopentanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
N-[4-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
N-[4-(4-phenylpiperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000055
N-[4-(4-pyridin-2-ylpiperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0057
N-[4-(aminomethyl)benzyl]-3-(5-[[[[(E)-2-phenylethenyl]sulfonyl](pyridin-2-ylmethyl)amino]methyl]-1,2,4-oxadiazol-3-yl)benzamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0013
N-[4-(piperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0019
N-[4-(pyrrolidine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.005
N-[4-methanesulfonylphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.058
N-[4-methoxyphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00067
N-[4-nitrophenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.026
N-[4-phenoxyphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.045
N-[4-toluyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0038
N-[4-trifluoromethylphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000034
N-[4-[4-(2-phenylcyclopropanecarbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00019
N-[4-[4-(2-trifluoromethylphenyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000025
N-[4-[4-(3-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00016
N-[4-[4-(3-phenylpropionyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00038
N-[4-[4-(3-phenylpropyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000052
N-[4-[4-(3-trifluoromethylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000041
N-[4-[4-(4,4-difluoropiperidine-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00031
N-[4-[4-(4-phenylbutyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000035
N-[4-[4-(6-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000076
N-[4-[4-(6-trifluoromethylpyridin-3-yl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00001
N-[4-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00002
N-[4-[4-(octahydroisoquinoline-2-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000026
N-[4-[4-(octahydroquinoline-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000037
N-[4-[4-(piperidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000057
N-[4-[4-(pyrrolidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
N-[5-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-pyridin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000015
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyridin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000014
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyrimidin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.03
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00021
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-ylmethyl]-carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00022
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-yl]-carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0015
[2-[(4-acryloylaminobenzenesulfonyl)methylamino]ethyl]-methylcarbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0029
[4-(4-acryloylpiperazine-1-sulfonyl)phenyl]carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
[4-[(4-aminophenyl)sulfonyl]piperazin-1-yl](cyclopropyl)methanone
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000273
(2-tert-butoxy-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0007
(2-[[(1R)-3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-1-carboxy-3-oxopropyl]amino]-2-oxoethyl)(dimethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0033
(2-[[4-(methoxycarbonyl)benzyl]oxy]-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0015
(2-[[6-(methoxycarbonyl)naphthalen-2-yl]methoxy]-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0015
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0036
(3E)-3-(2-oxopropylidene)-6-(trifluoromethoxy)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-3-[2-(3-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-3-[2-(4-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-3-[2-(5-bromopyridin-3-yl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.022
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3E)-4-chloro-1-(2-methylpropyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
(3E)-4-chloro-1-(cyclohexylmethyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.004
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
(3E)-4-chloro-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-chloro-3-[2-(2-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
(3E)-4-chloro-3-[2-(3-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3E)-4-chloro-3-[2-(3-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
(3E)-4-chloro-3-[2-(4-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-4-chloro-3-[2-(4-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-4-chloro-3-[2-(6-methoxypyridin-3-yl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-4-chloro-3-[2-oxo-2-(pyridin-2-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(2-phenylethyl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(3-phenylpropyl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(propan-2-yl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-phenyl-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
(3E)-4-chloro-3-[2-oxo-2-(pyridin-4-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0048
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0043
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.006
(3E)-5-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
(3E)-5-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0079
(3E)-5-nitro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-6-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.011
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0029
(3E)-7-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
(3E)-7-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0073
(3E)-7-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.018
(4R)-1-[(benzyloxy)carbonyl]-4-hydroxy-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.00044 - 0.00107
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
0.000029
(naphthalen-2-yl)methyl 4-[N-(bromoacetyl)glycyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.018
1,1'-methanediylbis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.25
1,1'-[(2,5-dimethylbenzene-1,4-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
Homo sapiens
-
IC50 above 0.25 mM, pH and temperature not specified in the publication
0.04
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.004
1,3-dimethyl-2-[(2-oxopropyl)thio]-1H-imidazol-3-ium
Homo sapiens
-
-
0.000875
1-(ethenylsulfonyl)tricyclo[3.3.1.13,7]decane
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000125
1-(tricyclo[3.3.1.13,7]dec-1-yl)prop-2-en-1-one
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.005
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.0009
2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl prop-2-enoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.1
2-([2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl]sulfanyl)-1,3,4,5-tetramethyl-1H-imidazol-3-ium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0000039
2-bromo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00000875
2-chloro-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0055
2-[(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]-N,N-dimethylacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.03
5,5'-methanediylbis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.025
5,5'-oxybis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.03 - 0.04
6,6'-oxybis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.005925
benzyl 4-[3-(acryloylamino)-2-oxopropanoyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.001725
benzyl 4-[3-[(ethenylsulfonyl)amino]-2-oxopropanoyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000889
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000775
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-ylmethoxy)ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00315
dimethyl[2-oxo-2-[2-(tricyclo[3.3.1.13,7]dec-1-yl)ethoxy]ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0018
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.009
GTP
Homo sapiens
-
-
0.1
indirubin
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.008
isoindigotin
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
methyl 3-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
methyl 4-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
methyl 4-[(acryloyloxy)methyl]benzoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0000021
methyl 4-[[(bromoacetyl)oxy]methyl]benzoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0021
methyl 6-[(acryloyloxy)methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000015
methyl 6-[[(bromoacetyl)oxy]methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00000665
methyl 6-[[(chloroacetyl)oxy]methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.011
methyl ketone
Homo sapiens
-
pH and temperature not specified in the publication
0.005
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
Homo sapiens
-
-
0.0000061
N-(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)prop-2-enamide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.11
N-(phenylcarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.3
N-(tert-butoxycarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.008
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.03
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.02
N-[(benzyloxy)carbonyl]-L-alanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.028
N-[(benzyloxy)carbonyl]-L-alpha-aspartyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.35
N-[(benzyloxy)carbonyl]-L-isoleucyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.003
N-[(benzyloxy)carbonyl]-L-phenylalanyl-5-oxo-6-[(1,3,4,5-tetramethyl-1H-imidazol-3-ium-2-yl)sulfanyl]-L-norleucine
Homo sapiens
-
-
0.02
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(diethylsulfonio)-5-oxo-L-norleucine
Homo sapiens
-
-
0.01
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.012
N-[(benzyloxy)carbonyl]-L-tryptophyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.008
N-[(benzyloxy)carbonyl]glycyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.15
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.00000629
tricyclo[3.3.1.13,7]dec-1-ylmethyl bromoacetate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.001625
tricyclo[3.3.1.13,7]dec-1-ylmethyl prop-2-enoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00038
[2-[(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)amino]-2-oxoethyl](dimethyl)sulfanium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00185
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](diethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0014
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](dimethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0013
-
epidermal transglutaminase
0.0037
-
plasma factor XIII
0.0072
-
platelet factor XIII
0.07
-
erythrocyte transglutaminase
0.156
-
tissue transglutaminase
2.5 - 3
-
-
8.7
-
pH 8.1, 37°C, enzyme enzyme expressed in apoplast
91.7
-
pH 8.1, 37°C, enzyme expressed in chloroplast
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
approx. value, hydrolysis reaction
6.5 - 7
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the transamidation reaction is kinetically favored over deamidation at pH-values above 7, but the deamidation reaction becomes kinetically competitive as the pH is lowered below 7 or as the concentration of amine substrates is lowered below their Km values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Caco-2 intestinal cancer cells express crosslinking-competent tTG on their surface
Manually annotated by BRENDA team
the central nervous system has a tTG splice variant which is termed tTG-short, or tTG-S. tTG-S adopts a conformation similar to the open-state
Manually annotated by BRENDA team
monocyte-derived, presence of large amounts of TG2 on cell surface
Manually annotated by BRENDA team
patients with Helicobacter pylori negative gastritis have higher t-TG activity than patients with healthy, unifected gastric mucosa
Manually annotated by BRENDA team
TG1 and TG2 are the most abundantly expressed TGs in normal kidney
Manually annotated by BRENDA team
monocyte-derived, presence of large amounts of TG2 on cell surface
Manually annotated by BRENDA team
presence of TG2 on cell surface in bowel tissue sections from both normal and celiac subjects
Manually annotated by BRENDA team
-
epidermal carcinoma cell line
Manually annotated by BRENDA team
-
enhanced serum immunoreactivity to tTG-2 antigens in some patients with multiple myeloma
Manually annotated by BRENDA team
-
MDA-MB-231 (doxorubicin resistant) human breast cancer cell
Manually annotated by BRENDA team
-
ex vivo cultures of nasal polyp mucosal explants of Cystic fibrosis patients and controls, cystic fibrosis transmembrane conductance regulator-defective IB3-1 bronchial epithelial cells, C38 isogenic CFTR corrected, and 16HBE normal bronchial epithelial cell lines. A defective cystic fibrosis transmembrane conductance regulator induces a remarkable up-regulation of tissue transglutaminase in both tissues and cell lines. The increased TG2 activity leads to functional sequestration of the anti-inflammatory peroxisome proliferator-activated receptor gamma and increase of the classic parameters of inflammation
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
-
cell line derived from human colon carcinoma
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
-
plasma factor XIII
Manually annotated by BRENDA team
-
3rd trimester of pregnancy
Manually annotated by BRENDA team
-
TGase activity in the basement membrane region
Manually annotated by BRENDA team
-
muscularis mucosae
Manually annotated by BRENDA team
-
isoform transglutaminase 2, both in patients with coeliac disease and controls. Enzyme is localized to subepithelial layer, lamina propria, and the pericryptal connective issue of all samples. It also binds to surface enterocytes of most untreated, but of few treated, coeliac patients, and shows no epithelial distribution in controls
Manually annotated by BRENDA team
-
primary foreskin fibroblast
Manually annotated by BRENDA team
-
isoform TG2 activity is eleveated in glioblastomas compared with non-neoplastic brain
Manually annotated by BRENDA team
follicle and cortex and cuticle of the hair shaft
Manually annotated by BRENDA team
-
leukemia cell line
Manually annotated by BRENDA team
TG1 and TG2 are the most abundantly expressed TGs in normal kidney
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
-
of the small bowel
Manually annotated by BRENDA team
-
of duodenum and colon
Manually annotated by BRENDA team
-
transglutaminase factor XIII levels are diminished in patients after infarct rupture. Transglutaminase factor XIII activity peaks on day 3 after myocardial infarction
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
-
TG2 expression promotes degradation of PTEN by ubiquitin-proteasomal pathway and results in constitutive activation of focal adhesion kinase/AKT cell survival signaling
Manually annotated by BRENDA team
-
PKCdelta plays an important role in regulation of TG2 expression in pancreatic ductal carcinoma cells and helps protect cells from autophagy, thus contributing to resistance to treatment
Manually annotated by BRENDA team
TG4 expression is restricted to the prostate gland
Manually annotated by BRENDA team
-
normal and glaucomatous cells express tissue transglutaminase 2. TGM2 protein levels and enzyme activities are elevated in glaucomatous cells
Manually annotated by BRENDA team
-
neuroblastoma SH-SY5Y cells
Manually annotated by BRENDA team
-
isoform tTG protein and RNA are present in stromal cells and trophoblasts of placenta in first trimester and at term, with higher levels later in pregnancy
Manually annotated by BRENDA team
-
isoform tTG protein and RNA are present in stromal cells and trophoblasts of placenta in first trimester and at term, with higher levels later in pregnancy
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
tTG and alpha-synuclein both localize to the endoplasmic reticulum in disease brain samples
Manually annotated by BRENDA team
intracellular TG1 activity is unlikely to contribute extracellularly to extracellular matrix crosslinking
Manually annotated by BRENDA team
additional information
-
expressed in apoplast and chloroplast
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
malfunction
metabolism
in general, TG-catalyzed crosslinking is the primary mechanism by which TGs promote disease progression
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TGM2_HUMAN
687
0
77329
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
x * 104000, GST and PreScission Protease-tagged enzyme, estimated from SDS-PAGE
77600
80240
recombinant His-tagged enzyme mutant G224V with bound GTP, gel filtration
28000
-
x * 82000, full length protein, x * 53000 + x * 28000, proteolytically processed N-terminal active fragment and C-terminal regulatory domain, respectively
280000 - 330000
-
plasma factor XIII, gel filtration and sedimentation equilibrium
53000
-
x * 82000, full length protein, x * 53000 + x * 28000, proteolytically processed N-terminal active fragment and C-terminal regulatory domain, respectively
55000
65000
-
gel filtration and sucrose density gradient centrifugation
71000
-
alpha2beta2, 4 * 71000, plasma factor XIIIa, alpha is the proteolytically modified catalytic subunit of factor XIII, SDS-PAGE
73183
-
x * 73183, factor XIII beta-subunit, deduced from nucleotide sequence
75000
77000
-
x * 77000, SDS-PAGE
78520
-
1 * 78520, including the C-terminal His-tag and GTP, calculated from amino acid sequence
78570
-
1 * 78570, multiangle light scattering
80000
82000
-
x * 82000, full length protein, x * 53000 + x * 28000, proteolytically processed N-terminal active fragment and C-terminal regulatory domain, respectively
83005
83010
-
primary structure
84000
-
x * 84000, recombinant transglutaminase 5, immunoblot
90000
-
recombinant transglutaminase 1, gel filtration
92000
-
1 * 92000, SDS-PAGE with or without 2-mercaptoethanol
additional information
-
TG2 can assume multiple conformations
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 80240, recombinant His-tagged enzyme mutant G224V with bound GTP, SDS-PAGE
monomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
-
membrane-bound enzyme of keratocytes is anchored via palmitate and myristate
phosphoprotein
-
phosphorylation of transglutaminase 2 (TG2) at serine-216 plays a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
proteolytic modification
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the enzyme inhibited with Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2, hanging-drop method at 25°C, 2 A resolution
human TG2 has been crystallized in its GDP- and GTP-bound form (PDB IDs 1KV3, 4PYG), in complex with ATP (PDB ID 3LY6), and with alternative inhibitors bound to its transamidase site within the alpha/beta-catalytic domain (PDB IDs 2Q3Z, 3S3J, 3S3P, 3S3S), structure modeling, analysis, overview
purified recombinant His-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris, pH 8.0, and 150 mM NaCl with 0.001 ml of reservoir solution containing 20 mM MES, pH 6.2, 150 mM sodium chloride, 5mM MgCl2, 4% PEG 3350, and 5 mM DTT, and 20% glycerol, equilibration against 0.4 ml of the reservoir solution, 20°C, X-ray diffraction structrue determination and analysis at 3.2 A resolution
hanging drop vapor diffusion method, using 20 mM MES at pH 6.8, 200 mM sodium chloride, 20 mM MgCl2, 6% (w/v) PEG 3350, 5 mM dithiothreitol, and 24% (v/v) glycerol
-
hanging drop vapour diffusion, 15 mg/ml transglutaminase 3, 0.1 mM beta-octylglucoside in 0.1 ml of enzyme in 20 mM Tris-HCl, pH 8.0, 1 mM EDTA, 125 mM NaCl and 3 mM CaCl2, well solution containing 4-12% polyethylene glycol 6K, 100 mM bicine, pH 9.0, and 1% dioxane at 21°C, X-ray structure of zymogen and activated transglutaminase 3 at 2.2 and 2.1 A resolution
in complex with guanosine 5’-O-(thiotriphosphate) and with GDP
-
in presence of Ca2+ and/or Mg2+
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C277A
the mutant is unable to bind guanine nucleotides
C277S
the mutation has no effect on cell death
C277V
the mutant is susceptible to digestion by trypsin, and significantly impaired in nucleotide binding
D306N/N310A
the purified tTG mutant adopts a conformation similar to that of wild-type tTG, based on their mutual ability to bind bodipy-GTP-gammaS and to resist proteolysis by trypsin
D434A
the mutant can be transiently expressed in NIH 3T3 cells but not be generated as recombinant protein. The mutant is cytotoxic when expressed in NIH 3T3 cells
F174A
the F174A mutant is deficient in nucleotide binding, and is digested by trypsin in the presence of GTP-gammaS, Phe174 appears to be involved in a pi-stacking interaction
F174W
mutant resists proteolysis and is able to bind nucleotide
G224V
K677A
the mutant can be transiently expressed in NIH 3T3 cells but not be generated as recombinant protein, the mutant is unable to bind bodipy-GTP-gammaS, and shows high sensitivity to degradation by trypsin. The mutant is cytotoxic when expressed in NIH 3T3 cells
N681A
the mutant can be transiently expressed in NIH 3T3 cells and generated as recombinant protein. The mutant is cytotoxic when expressed in NIH 3T3 cells
Q163D
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q163L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q164L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q169L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
R476A
the mutant binds nucleotide as well as the wild-type enzyme
R478A
the mutant has partially reduced nucleotide binding
R579A
the R579A mutant of tTG is far more susceptible to proteolysis by trypsin or by calpain than the wild-type
R580A
the mutant is GTP-binding deficient
R580K
decreases in nucleotide binding are observed for the R580L and R580K mutants
R580L
decreases in nucleotide binding are observed for the R580L and R580K mutants
R580L/C277A
the tTG mutant is deficient in GTP-binding and protein crosslinking activity, but still induces cell death
S171A
the mutant binds nucleotide as well as the wild-type enzyme
T360A
mutants show an increase in preference for deamidation with respect to transamidation compared to the wild-type enzyme
T360W
mutants show an increase in preference for deamidation with respect to transamidation compared to the wild-type enzyme
W241A
no detectable activity
W254A
the mutant can be transiently expressed in NIH 3T3 cells and generated as recombinant protein, the mutant is unable to bind bodipy-GTP-gammaS, and shows high sensitivity to degradation by trypsin. W254A forms a dimer of tTG molecules in the open-state conformation. The mutant is cytotoxic when expressed in NIH 3T3 cells
W332A
no detectable activity
Y516C
the mutant is less capable of binding guanine nucleotide compared to wild-type
Y516F
the mutant is less capable of binding guanine nucleotide compared to wild-type
C230A
-
the mutant shows about wild type activity but is less susceptible to oxidation than the wild type enzyme
C277S
C370A
-
the kcat/Km is 33% of the wild type enzyme
C371A
-
the kcat/Km is 5% of the wild type enzyme
D151N/E153Q/E154Q/E155Q/E158Q
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity. GTPase activity is activated by presence of Ca2+
D306N/N308S/N310S
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
D434N/E435Q/E437N
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity. GTPase activity is activated by presence of Ca2+
E396Q/N398S/D400N
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
E447Q/E451Q/E452Q/E454Q
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
N229S/N231S/D232N/D233N
-
mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
S216A
-
the mutant lacks the S216 phosphorylation site
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
t1/2: 1-2 min stable at 37°C, at least 20 min stable at 4°C
487831
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
melting temperature
37
-
t1/2: 1-2 min, pH 9.0
4
-
at least 20 min stable, pH 9.0
56
-
heating in the presence of Ca2+ increases activity 25-fold, human epidermal enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
gel electrophoresis inactivates
-
repeated freeze-thawing results in some loss of activity, dithothreitol restores activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethylformamide
about 90% activity at 2.5 and 5.0 mM dimethylformamide
DMSO
100% activity in the presence of 2.5 and 5.0 mM DMSO
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is reversibly inactivated by oxidation
-
719877
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified enzyme, 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0, several months, no loss of activity
4°C, lyophilised purified enzyme, 1 week, 80% loss of activity
4°C, purified enzyme, 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0, 1 week, 10% loss of activity
4°C, purified enzyme, 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0, 2 weeks, 25% loss of activity
-30°C, human zymogen factor XIII, over 1 year
-
-30°C, lyophilized human zymogen factor XIII, several years
-
4°C, 50 mM Tris, pH 7.5, 1 mM EDTA/0.5 mM DTT, up to 2 weeks, no loss of activity
-
4°C, at least 4 months
-
4°C, epidermal transglutaminase, at least 1 month
-
dilute enzyme solutions are unstable to storage at 4°C
-
human factor XIIIa is more stable to storage, when Ca2+ is omitted
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose 4B resin chromatography
glutathione Sepharose column chromatography
Ni-NTA column chromatography
recombinant GST-tagged full-length TG2 V224 and G224 variants from Escherichia coli strain Rosetta 2 (DE3) by glutathione affinity chromatography
recombinant His-tagged full-length wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gelfiltration, followed by anion exchange chromatography, a second step of gel filtration, and ultrafiltration
TALON resin column chromatography and Superdex 200 gel filtration
2 forms of epidermal enzyme
-
cytosolic tissue transglutaminase, DE52, heparin-agarose, casein-agarose
-
epidermal transglutaminase, DEAE-cellulose, Sephadex G-75, CM-cellulose, gel filtration
-
erythrocyte transglutaminase
-
erythrocyte transglutaminase, DE-52 gel, Sephacryl S-300, Blue Sepharose, DEAE bio-gel
-
erythrocyte transglutaminase, DEAE cellulose, AcA 44, heparin-Sepharose, gel filtration
-
Ni-NTA affinity resin column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography and HiTrap Q column chromatography
-
partial
-
plasma factor XIII, BaCl2, glycine, heat treatment, gel filtration, platelet factor XIII, DEAE-cellulose, hydroxyapatite
-
recombinant factor XIII-tissue transglutaminase chimeras
-
recombinant transglutaminase 1, DEAE-Sephacel, heparin-Sepharose, gel filtration
-
transglutaminase C
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta 2 (DE3) cells
expressed in Escherichia coli Rosetta 2 cells
recombinant expression of enzyme mutants in HeLa cells and in NIH 3T3 fibroblasts, nearly half of the cells die within 24 h. In contrast, introduction of wild-type tTG into those same cells does not induce cell death. Mutant R580L/C277A still induces cell death. Although ectopic expression of tTG mutant R580A in striatal cells is not sufficient to induce cell death, it does so in HeLa or NIH 3T3 cells
recombinant expression of GST-tagged full-length TG2 V224 and truncated G224 variants in Escherichia coli strain Rosetta 2 (DE3)
recombinant expression of His-tagged full-length wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
cloning of factor XIII beta-subunit cDNA
-
cloning of factor XIII-tissue transglutaminase chimeras in Escherichia coli
-
cloning of placenta FXIIIa-gene cDNA
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli Rosetta 2 pLysS cells
-
expression in SH-SY5Y, SK-N-SH, A172, U373MG, HeLa, MCF7 and HEK293 cells
-
expression of transglutaminase 1 in Sf9 insect cells
-
expression of transglutaminase 3 in Sf9 cells
factor XIII, transglutaminase C and transglutaminase K
-
isoform TGase 1
-
transfection of HaCat cell and HEK-293 cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
antral t-TG activity is significantly increased in Helicobacter pylori positive patients compared to Helicobacter pylori negative patients. The activity of t-TG is higher in patients harboring cagA positive strains vs. cagA negative strains
enzyme expression is up-regulated in the brains of Huntington’s disease patients
enzyme expression is significantly lower in melanoma cells than in control keratinocytes
-
hypoxia induces TG2 expression through an HIF-1 dependent pathway and concurrently activates intracellular TG2
-
the enzyme plays a key role in homocysteine-induced activation of THP-1 monocytes, involving oxidative as well as endoplasmic resticulum stress and inflammation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
tTG is considered a prognostic marker for Parkinson's disease. tTG antibodies, and crosslinked gliadin, act as diagnostic tools in celiac disease
analysis
-
specific tests for measuring the activities of TGase 1 and factor XIII based on their ability to incorporate biotinylated peptides onto spermine-conjugated wells. The rapid and sensitive colorimetric assay shows high sensitivity when TGase isozymes are assayed using their identified preferred substrate peptide. The limit of detection for factor XIII and TGase 1 is as low as 0.01 mU/ml. In each case, good linearity is obtained
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takahashi, N.; Takahashi, Y.; Putnam, F.W.
Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta
Proc. Natl. Acad. Sci. USA
83
8019-8023
1986
Homo sapiens
Manually annotated by BRENDA team
Lee, K.N.; Birckbichler, P.J.; Patterson, M.K.
GTP hydrolysis by guinea pig liver transglutaminase
Biochem. Biophys. Res. Commun.
162
1370-1375
1989
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Ando, Y.; Imamura, S.; Yamagata, Y.; Kikuchi, T.; Murachi, T.; Kannagi, R.
High-performance liquid chromatographic assay of transglutaminase and its application to the purification of human erythrocyte transglutaminase and platelet factor XIII
J. Biochem.
101
1331-1337
1987
Homo sapiens
Manually annotated by BRENDA team
Signorini, M.; Bortolotti, F.; Poltronieri, L.; Bergamini, C.M.
Human erythrocyte transglutaminase: purification and preliminary characterisation
Biol. Chem. Hoppe-Seyler
369
275-281
1988
Homo sapiens
Manually annotated by BRENDA team
Puzkin, E.G.; Raghuraman, V.
Catalytic properties of a calmodulin-regulated transglutaminase from human platelet and chicken gizzard
J. Biol. Chem.
260
16012-16020
1985
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Parameswaran, K.N.; Velasco, P.T.; Wilson, J.; Lorand, L.
Labeling of epsilon-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase
Proc. Natl. Acad. Sci. USA
87
8472-8475
1990
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Jensen, P.H.; Lorand, L.; Ebbesen, P.; Gliemann, J.
Type-2 plasminogen-activator inhibitor is a substrate for trophoblast transglutaminase and factor XIIIa. Transglutaminase-catalyzed cross-linking to cellular and extracellular structures
Eur. J. Biochem.
214
141-146
1993
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Achyuthan, K.E.; Mary, A.; Greenberg, C.S.
Tb(III)-ion-binding-induced conformational changes in platelet factor XIII
Biochem. J.
257
331-338
1989
Homo sapiens
Manually annotated by BRENDA team
Greenberg, C.S.; Birckbichler, P.J.; Rice, R.H.
Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues
FASEB J.
5
3071-3077
1991
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Dadabay, C.Y.; Pike, L.J.
Purification and characterization of a cytosolic transglutaminase from a cultured human tumour-cell line
Biochem. J.
264
679-685
1989
Homo sapiens
Manually annotated by BRENDA team
Bergamini, C.M.; Signorini, M.; Poltronieri, L.
Inhibition of erythrocyte transglutaminase by GTP
Biochim. Biophys. Acta
916
149-151
1987
Homo sapiens
Manually annotated by BRENDA team
Folk, J.E.; Chung, S.I.
Transglutaminases
Methods Enzymol.
113
358-375
1985
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Ichinose, A.; Bottenus, R.E.; Davie, E.W.
Structure of transglutaminases
J. Biol. Chem.
265
13411-13414
1990
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Kawashima, S.
Inhibition of rat liver transglutaminase by nucleotides
Experientia
47
709-712
1991
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Negi, M.; Colbert, M.C.; Goldsmith, L.A.
High-molecular-weight human epidermal transglutaminase
J. Invest. Dermatol.
85
75-78
1985
Homo sapiens
Manually annotated by BRENDA team
Chang, S.K.; Chung, S.I.
Cellular transglutaminase. The particulate-associated transglutaminase from chondrosarcoma and liver: partial purification and characterization
J. Biol. Chem.
261
8112-8121
1986
Cavia porcellus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Folk, J.E.; Chung, S.I.
Molecular and catalytic properties of transglutaminases
Adv. Enzymol. Relat. Areas Mol. Biol.
38
109-191
1973
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
McCormack, S.A.; Wang, J.Y.; Viar, M.J.; Tague, L.; Davies, P.J.A.; Johnson, L.R.
Polyamines influence transglutaminase activity and cell migration in two cell lines
Am. J. Physiol.
267
C706-C714
1994
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hettasch, J.M.; Peoples, K.A.; Greenberg, C.S.
Analysis of factor XIII substrate specificity using recombinant human factor XIII and tissue transglutaminase chimeras
J. Biol. Chem.
272
25149-25156
1997
Homo sapiens
Manually annotated by BRENDA team
Murthy, S.N.P.; Velasco, P.T.; Lorand, L.
Properties of purified lens transglutaminase and regulation of its transamidase/crosslinking activity by GTP
Exp. Eye Res.
67
273-281
1998
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Zhang, J.; Guttmann, R.P.; Johnson, G.V.W.
Tissue transglutaminase is an in situ substrate of calpain: regulation of activity
J. Neurochem.
71
240-247
1998
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Hitomi, K.; Yamagiwa, Y.; Ikura, K.; Yamanishi, K.; Maki, M.
Characterization of human recombinant transglutaminase 1 purified from baculovirus-infected insect cells
Biosci. Biotechnol. Biochem.
64
2128-2137
2000
Homo sapiens
Manually annotated by BRENDA team
Candi, E.; Oddi, S.; Terrinoni, A.; Paradisi, A.; Ranalli, M.; Finazzi-Agro, A.; Melino, G.
Transglutaminase 5 cross-links loricrin, involucrin, and small proline-rich proteins in vitro
J. Biol. Chem.
276
35014-35023
2001
Homo sapiens
Manually annotated by BRENDA team
Ruse, M.; Lambert, A.; Robinson, N.; Ryan, D.; Shon, K.J.; Eckert, R.L.
S100A7, S100A10, and S100A11 are transglutaminase substrates
Biochemistry
40
3167-3173
2001
Homo sapiens
Manually annotated by BRENDA team
Griffin, M.; Casadio, R.; Bergamini, C.M.
Transglutaminases: Nature's biological glues
Biochem. J.
368
377-396
2002
Mammalia, Rattus norvegicus, Homo sapiens (P21980)
Manually annotated by BRENDA team
Ahvazi, B.; Kim, H.C.; Kee, S.H.; Nemes, Z.; Steinert, P.M.
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation
EMBO J.
21
2055-2067
2002
Homo sapiens (Q08188), Homo sapiens
Manually annotated by BRENDA team
Case, A.; Stein, R.L.
Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates
Biochemistry
42
9466-9481
2003
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Jeon, J.H.; Lee, H.J.; Jang, G.Y.; Kim, C.W.; Shim, D.M.; Cho, S.Y.; Yeo, E.J.; Park, S.C.; Kim, I.G.
Different inhibition characteristics of intracellular transglutaminase activity by cystamine and cysteamine
Exp. Mol. Med.
36
576-581
2004
Homo sapiens
Manually annotated by BRENDA team
D'Argenio, G.; Calvani, M.; Della Valle, N.; Cosenza, V.; Di Matteo, G.; Giorgio, P.; Margarucci, S.; Petillo, O.; Jori, F.P.; Galderisi, U.; Peluso, G.
Differential expression of multiple transglutaminases in human colon: Impaired keratinocyte transglutaminase expression in ulcerative colitis
Gut
54
496-502
2005
Homo sapiens
Manually annotated by BRENDA team
Sorrentino, A.; Schillberg, S.; Fischer, R.; Rao, R.; Porta, R.; Mariniello, L.
Recombinant human tissue transglutaminase produced into tobacco suspension cell cultures is active and recognizes autoantibodies in the serum of celiac patients
Int. J. Biochem. Cell Biol.
37
842-851
2005
Homo sapiens
Manually annotated by BRENDA team
Ahvazi, B.; Boeshans, K.M.; Idler, W.; Baxa, U.; Steinert, P.M.
Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme
J. Biol. Chem.
278
23834-23841
2003
Homo sapiens (Q08188)
Manually annotated by BRENDA team
Shin, D.M.; Jeon, J.H.; Kim, C.W.; Cho, S.Y.; Kwon, J.C.; Lee, H.J.; Choi, K.H.; Park, S.C.; Kim, I.G.
Cell Type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis
J. Biol. Chem.
279
15032-15039
2004
Homo sapiens
Manually annotated by BRENDA team
Rodolfo, C.; Mormone, E.; Matarrese, P.; Ciccosanti, F.; Farrace, M.G.; Garofano, E.; Piredda, L.; Fimia, G.M.; Malorni, W.; Piacentini, M.
Tissue transglutaminase is a multifunctional BH3-only protein
J. Biol. Chem.
279
54783-54792
2004
Homo sapiens
Manually annotated by BRENDA team
Ahvazi, B.; Boeshans, K.M.; Idler, W.; Baxa, U.; Steinert, P.M.; Rastinejad, F.
Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium
J. Biol. Chem.
279
7180-7192
2004
Homo sapiens
Manually annotated by BRENDA team
Stephens, P.; Grenard, P.; Aeschlimann, P.; Langley, M.; Blain, E.; Errington, R.; Kipling, D.; Thomas, D.; Aeschlimann, D.
Crosslinking and G-protein functions of transglutaminase 2 contribute differentially to fibroblast wound healing responses
J. Cell Sci.
117
3389-3403
2004
Homo sapiens
Manually annotated by BRENDA team
Case, A.; Stein, R.L.
Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor
Biochemistry
46
1106-1115
2007
Homo sapiens
Manually annotated by BRENDA team
Cleary, D.B.; Maurer, M.C.
Characterizing the specificity of activated Factor XIII for glutamine-containing substrate peptides
Biochim. Biophys. Acta
1764
1207-1217
2006
Homo sapiens
Manually annotated by BRENDA team
Duval, E.; Case, A.; Stein, R.L.; Cuny, G.D.
Structure-activity relationship study of novel tissue transglutaminase inhibitors
Bioorg. Med. Chem. Lett.
15
1885-1889
2005
Homo sapiens
Manually annotated by BRENDA team
Choi, K.; Siegel, M.; Piper, J.L.; Yuan, L.; Cho, E.; Strnad, P.; Omary, B.; Rich, K.M.; Khosla, C.
Chemistry and biology of dihydroisoxazole derivatives: selective inhibitors of human transglutaminase 2
Chem. Biol.
12
469-475
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Biagi, F.; Campanella, J.; Laforenza, U.; Gastaldi, G.; Tritto, S.; Grazioli, M.; Villanacci, V.; Corazza, G.R.
Transglutaminase 2 in the enterocytes is coeliac specific and gluten dependent
Dig. Liver Dis.
38
652-658
2006
Homo sapiens
Manually annotated by BRENDA team
Sugimura, Y.; Hosono, M.; Wada, F.; Yoshimura, T.; Maki, M.; Hitomi, K.
Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA
J. Biol. Chem.
281
17699-17706
2006
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Janiak, A.; Zemskov, E.A.; Belkin, A.M.
Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway
Mol. Biol. Cell
17
1606-1619
2006
Homo sapiens
Manually annotated by BRENDA team
Yuan, L.; Siegel, M.; Choi, K.; Khosla, C.; Miller, C.R.; Jackson, E.N.; Piwnica-Worms, D.; Rich, K.M.
Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy
Oncogene
26
2563-2573
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Robinson, N.J.; Glazier, J.D.; Greenwood, S.L.; Baker, P.N.; Aplin, J.D.
Tissue transglutaminase expression and activity in placenta
Placenta
27
148-157
2005
Homo sapiens
Manually annotated by BRENDA team
Eckert, R.L.; Sturniolo, M.T.; Jans, R.; Kraft, C.A.; Jiang, H.; Rorke, E.A.
TIG3: a regulator of type I transglutaminase activity in epidermis
Amino Acids
36
739-746
2009
Homo sapiens
Manually annotated by BRENDA team
Griffin, M.; Mongeot, A.; Collighan, R.; Saint, R.E.; Jones, R.A.; Coutts, I.G.; Rathbone, D.L.
Synthesis of potent water-soluble tissue transglutaminase inhibitors
Bioorg. Med. Chem. Lett.
18
5559-5562
2008
Homo sapiens
Manually annotated by BRENDA team
Juranic, Z.; Radic, J.; Konic-Ristic, A.; Jelic, S.; Mihaljevic, B.; Stankovic, I.; Matkovic, S.; Besu, I.; Gavrilovic, D.
Humoral immunoreactivity to gliadin and to tissue transglutaminase is present in some patients with multiple myeloma
BMC Immunol.
9
22
2008
Homo sapiens
Manually annotated by BRENDA team
Harrison, C.A.; Layton, C.M.; Hau, Z.; Bullock, A.J.; Johnson, T.S.; MacNeil, S.
Transglutaminase inhibitors induce hyperproliferation and parakeratosis in tissue-engineered skin
Br. J. Dermatol.
156
247-257
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, D.S.; Park, K.S.; Jeong, K.C.; Lee, B.I.; Lee, C.H.; Kim, S.Y.
Glucosamine is an effective chemo-sensitizer via transglutaminase 2 inhibition
Cancer Lett.
273
243-249
2008
Homo sapiens
Manually annotated by BRENDA team
Kawai, Y.; Wada, F.; Sugimura, Y.; Maki, M.; Hitomi, K.
Transglutaminase 2 activity promotes membrane resealing after mechanical damage in the lung cancer cell line A549
Cell Biol. Int.
32
928-934
2008
Homo sapiens
Manually annotated by BRENDA team
Lai, T.S.; Liu, Y.; Tucker, T.; Daniel, K.R.; Sane, D.C.; Toone, E.; Burke, J.R.; Strittmatter, W.J.; Greenberg, C.S.
Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries
Chem. Biol.
15
969-978
2008
Homo sapiens
Manually annotated by BRENDA team
Verma, A.; Guha, S.; Wang, H.; Fok, J.Y.; Koul, D.; Abbruzzese, J.; Mehta, K.
Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells
Clin. Cancer Res.
14
1997-2005
2008
Homo sapiens
Manually annotated by BRENDA team
Nahrendorf, M.; Aikawa, E.; Figueiredo, J.L.; Stangenberg, L.; van den Borne, S.W.; Blankesteijn, W.M.; Sosnovik, D.E.; Jaffer, F.A.; Tung, C.H.; Weissleder, R.
Transglutaminase activity in acute infarcts predicts healing outcome and left ventricular remodelling: implications for FXIII therapy and antithrombin use in myocardial infarction
Eur. Heart J.
29
445-454
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Shin, D.M.; Jeon, J.H.; Kim, C.W.; Cho, S.Y.; Lee, H.J.; Jang, G.Y.; Jeong, E.M.; Lee, D.S.; Kang, J.H.; Melino, G.; Park, S.C.; Kim, I.G.
TGFbeta mediates activation of transglutaminase 2 in response to oxidative stress that leads to protein aggregation
FASEB J.
22
2498-2507
2008
Homo sapiens
Manually annotated by BRENDA team
Tovar-Vidales, T.; Roque, R.; Clark, A.F.; Wordinger, R.J.
Tissue transglutaminase expression and activity in normal and glaucomatous human trabecular meshwork cells and tissues
Invest. Ophthalmol. Vis. Sci.
49
622-628
2008
Homo sapiens
Manually annotated by BRENDA team
Cabrera-Chavez, F.; Rouzaud-Sandez, O.; Sotelo-Cruz, N.; Calderon de la Barca, A.M.
Transglutaminase treatment of wheat and maize prolamins of bread increases the serum IgA reactivity of celiac disease patients
J. Agric. Food Chem.
56
1387-1391
2008
Homo sapiens
Manually annotated by BRENDA team
Hartley, D.M.; Zhao, C.; Speier, A.C.; Woodard, G.A.; Li, S.; Li, Z.; Walz, T.
Transglutaminase induces protofibril-like amyloid beta-protein assemblies that are protease-resistant and inhibit long-term potentiation
J. Biol. Chem.
283
16790-16800
2008
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Maiuri, L.; Luciani, A.; Giardino, I.; Raia, V.; Villella, V.R.; DApolito, M.; Pettoello-Mantovani, M.; Guido, S.; Ciacci, C.; Cimmino, M.; Cexus, O.N.; Londei, M.; Quaratino, S.
Tissue transglutaminase activation modulates inflammation in cystic fibrosis via PPARgamma down-regulation
J. Immunol.
180
7697-7705
2008
Homo sapiens
Manually annotated by BRENDA team
Gupta, M.; Greenberg, C.S.; Eckman, D.M.; Sane, D.C.
Arterial vimentin is a transglutaminase substrate: a link between vasomotor activity and remodeling?
J. Vasc. Res.
44
339-344
2007
Homo sapiens
Manually annotated by BRENDA team
Akar, U.; Ozpolat, B.; Mehta, K.; Fok, J.; Kondo, Y.; Lopez-Berestein, G.
Tissue transglutaminase inhibits autophagy in pancreatic cancer cells
Mol. Cancer Res.
5
241-249
2007
Homo sapiens
Manually annotated by BRENDA team
Siegel, M.; Khosla, C.
Transglutaminase 2 inhibitors and their therapeutic role in disease states
Pharmacol. Ther.
115
232-245
2007
Cavia porcellus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Pinkas, D.M.; Strop, P.; Brunger, A.T.; Khosla, C.
Transglutaminase 2 undergoes a large conformational change upon activation
PLoS Biol.
5
e327
2007
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Chen, C.S.; Wu, C.H.; Lai, Y.C.; Lee, W.S.; Chen, H.M.; Chen, R.J.; Chen, L.C.; Ho, Y.S.; Wang, Y.J.
NF-kappaB-activated tissue transglutaminase is involved in ethanol-induced hepatic injury and the possible role of propolis in preventing fibrogenesis
Toxicology
246
148-157
2008
Homo sapiens
Manually annotated by BRENDA team
Hitomi, K.; Kitamura, M.; Alea, M.P.; Ceylan, I.; Thomas, V.; El Alaoui, S.
A specific colorimetric assay for measuring transglutaminase 1 and factor XIII activities
Anal. Biochem.
394
281-283
2009
Homo sapiens
Manually annotated by BRENDA team
Kiraly, R.; Csosz, E.; Kurtan, T.; Antus, S.; Szigeti, K.; Simon-Vecsei, Z.; Korponay-Szabo, I.R.; Keresztessy, Z.; Fesues, L.
Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis
FEBS J.
276
7083-7096
2009
Homo sapiens
Manually annotated by BRENDA team
Hodrea, J.; Demeny, M.A.; Majai, G.; Sarang, Z.; Korponay-Szabo, I.R.; Fesues, L.
Transglutaminase 2 is expressed and active on the surface of human monocyte-derived dendritic cells and macrophages
Immunol. Lett.
130
74-81
2010
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Satpathy, M.; Shao, M.; Emerson, R.; Donner, D.B.; Matei, D.
Tissue transglutaminase regulates matrix metalloproteinase-2 in ovarian cancer by modulating cAMP-response element-binding protein activity
J. Biol. Chem.
284
15390-15399
2009
Homo sapiens
Manually annotated by BRENDA team
Yi, S.J.; Groffen, J.; Heisterkamp, N.
Transglutaminase 2 regulates the GTPase-activating activity of Bcr
J. Biol. Chem.
284
35645-35651
2009
Homo sapiens
Manually annotated by BRENDA team
Zeugolis, D.I.; Panengad, P.P.; Yew, E.S.; Sheppard, C.; Phan, T.T.; Raghunath, M.
An in situ and in vitro investigation for the transglutaminase potential in tissue engineering
J. Biomed. Mater. Res. A
92
1310-1320
2010
Homo sapiens
Manually annotated by BRENDA team
Pietroni, V.; Di Giorgi, S.; Paradisi, A.; Ahvazi, B.; Candi, E.; Melino, G.
Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells
J. Invest. Dermatol.
128
2760-2766
2008
Homo sapiens
Manually annotated by BRENDA team
Csosz, E.; Bagossi, P.; Nagy, Z.; Dosztanyi, Z.; Simon, I.; Fesus, L.
Substrate preference of transglutaminase 2 revealed by logistic regression analysis and intrinsic disorder examination
J. Mol. Biol.
383
390-402
2008
Homo sapiens
Manually annotated by BRENDA team
Jang, G.Y.; Jeon, J.H.; Cho, S.Y.; Shin, D.M.; Kim, C.W.; Jeong, E.M.; Bae, H.C.; Kim, T.W.; Lee, S.H.; Choi, Y.; Lee, D.S.; Park, S.C.; Kim, I.G.
Transglutaminase 2 suppresses apoptosis by modulating caspase 3 and NF-kappaB activity in hypoxic tumor cells
Oncogene
29
356-367
2010
Homo sapiens
Manually annotated by BRENDA team
Lai, T.S.; Davies, C.; Greenberg, C.S.
Human tissue transglutaminase is inhibited by pharmacologic and chemical acetylation
Protein Sci.
19
229-235
2010
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Facchiano, F.; DArcangelo, D.; Lentini, A.; Rossi, S.; Senatore, C.; Pannellini, T.; Tabolacci, C.; Facchiano, A.M.; Facchiano, A.; Beninati, S.
Tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination: an in vivo study
Amino Acids
44
53-61
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kloeck, C.; Jin, X.; Choi, K.; Khosla, C.; Madrid, P.B.; Spencer, A.; Raimundo, B.C.; Boardman, P.; Lanza, G.; Griffin, J.H.
Acylideneoxoindoles: a new class of reversible inhibitors of human transglutaminase 2
Bioorg. Med. Chem. Lett.
21
2692-2696
2011
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Ande, S.R.; Mishra, S.
Phosphorylation of transglutaminase 2 (TG2) at serine-216 plays a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN
BMC Cancer
12
277
2012
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Stamnaes, J.; Pinkas, D.M.; Fleckenstein, B.; Khosla, C.; Sollid, L.M.
Redox regulation of transglutaminase 2 activity
J. Biol. Chem.
285
25402-25409
2010
Homo sapiens
Manually annotated by BRENDA team
Prime, M.E.; Andersen, O.A.; Barker, J.J.; Brooks, M.A.; Cheng, R.K.; Toogood-Johnson, I.; Courtney, S.M.; Brookfield, F.A.; Yarnold, C.J.; Marston, R.W.; Johnson, P.D.; Johnsen, S.F.; Palfrey, J.J.; Vaidya, D.; Erfan, S.; Ichihara, O.; Felicetti, B.; Palan, S.; Pedret-Dunn, A.; Schaertl, S.; Sternberger, I.
Discovery and structure-activity relationship of potent and selective covalent inhibitors of transglutaminase 2 for Huntingtons disease
J. Med. Chem.
55
1021-1046
2012
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Roy, I.; Smith, O.; Clouthier, C.M.; Keillor, J.W.
Expression, purification and kinetic characterisation of human tissue transglutaminase
Protein Expr. Purif.
87
41-46
2013
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Kanchan, K.; Erguelen, E.; Kiraly, R.; Simon-Vecsei, Z.; Fuxreiter, M.; Fesues, L.
Identification of a specific one amino acid change in recombinant human transglutaminase 2 that regulates its activity and calcium sensitivity
Biochem. J.
455
261-272
2013
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Piacentini, M.; DEletto, M.; Farrace, M.G.; Rodolfo, C.; Del Nonno, F.; Ippolito, G.; Falasca, L.
Characterization of distinct sub-cellular location of transglutaminase type II: changes in intracellular distribution in physiological and pathological states
Cell Tissue Res.
358
793-805
2014
Homo sapiens
Manually annotated by BRENDA team
Badarau, E.; Wang, Z.; Rathbone, D.L.; Costanzi, A.; Thibault, T.; Murdoch, C.E.; El Alaoui, S.; Bartkeviciute, M.; Griffin, M.
Development of potent and selective tissue transglutaminase inhibitors: their effect on TG2 function and application in pathological conditions
Chem. Biol.
22
1347-1361
2015
Homo sapiens
Manually annotated by BRENDA team
Karashima, T.; Furumura, M.; Ishii, N.; Ohyama, B.; Saruta, H.; Natsuaki, Y.; Nakama, T.; Ohata, C.; Tsuruta, D.; Hitomi, K.; Hashimoto, T.
Distinct protein expression and activity of transglutaminases found in different epidermal tumors
Exp. Dermatol.
23
433-435
2014
Homo sapiens
Manually annotated by BRENDA team
Curro, M.; Gangemi, C.; Gugliandolo, A.; Risitano, R.; Ferlazzo, N.; Ientile, R.; Caccamo, D.
Transglutaminase 2 is involved in homocysteine-induced activation of human THP-1 monocytes
Free Radic. Res.
49
299-308
2015
Homo sapiens
Manually annotated by BRENDA team
Kloeck, C.; Herrera, Z.; Albertelli, M.; Khosla, C.
Discovery of potent and specific dihydroisoxazole inhibitors of human transglutaminase 2
J. Med. Chem.
57
9042-9064
2014
Homo sapiens
Manually annotated by BRENDA team
Fang, J.Y.; Tan, S.J.; Yang, Z.; Tayag, C.; Han, B.
Tumor bioengineering using a transglutaminase crosslinked hydrogel
PLoS ONE
9
e105616
2014
Homo sapiens
Manually annotated by BRENDA team
Zhuang, R.; Khosla, C.
Substrates, inhibitors, and probes of mammalian transglutaminase 2
Anal. Biochem.
591
113560
2020
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Wells, E.A.; Anderson, M.A.; Zeczycki, T.N.
15(V/K) kinetic isotope effect and steady-state kinetic analysis for the transglutaminase 2 catalyzed deamidation and transamidation reactions
Arch. Biochem. Biophys.
643
57-61
2018
Homo sapiens (P21980)
Manually annotated by BRENDA team
Yamane, M.; Sugimura, K.; Kawasaki, H.; Tatsukawa, H.; Hitomi, K.
Analysis on transglutaminase 1 and its substrates using specific substrate peptide in cultured keratinocytes
Biochem. Biophys. Res. Commun.
478
343-348
2016
Homo sapiens (P22735)
Manually annotated by BRENDA team
Erguelen, E.; Becsi, B.; Csomos, I.; Fesues, L.; Kanchan, K.
Identification of DNAJA1 as a novel interacting partner and a substrate of human transglutaminase 2
Biochem. J.
473
3889-3901
2016
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Pina Dore, M.; Pes, G.M.; Errigo, A.; Manca, A.; Realdi, G.
Tissue transglutaminase activity in human gastric mucosa according to Helicobacter pylori infection
Exp. Biol. Med. (Maywood)
243
1161-1164
2018
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team
Lorand, L.; Iismaa, S.E.
Transglutaminase diseases from biochemistry to the bedside
FASEB J.
33
3-12
2019
Homo sapiens (O43548), Homo sapiens (O95932), Homo sapiens (P16452), Homo sapiens (P21980), Homo sapiens (P22735), Homo sapiens (P49221), Homo sapiens (Q08188), Homo sapiens (Q96PF1), Homo sapiens, Mus musculus (P21981), Mus musculus (Q9JLF6)
Manually annotated by BRENDA team
Akbar, A.; McNeil, N.M.R.; Albert, M.R.; Ta, V.; Adhikary, G.; Bourgeois, K.; Eckert, R.L.; Keillor, J.W.
Structure-activity relationships of potent, targeted covalent inhibitors that abolish both the transamidation and GTP binding activities of human tissue transglutaminase
J. Med. Chem.
60
7910-7927
2017
Homo sapiens
Manually annotated by BRENDA team
Wodtke, R.; Hauser, C.; Ruiz-Gomez, G.; Jaeckel, E.; Bauer, D.; Lohse, M.; Wong, A.; Pufe, J.; Ludwig, F.A.; Fischer, S.; Hauser, S.; Greif, D.; Pisabarro, M.T.; Pietzsch, J.; Pietsch, M.; Loeser, R.
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2 synthesis, structure-activity relationships, and pharmacokinetic profiling
J. Med. Chem.
61
4528-4560
2018
Cavia porcellus (H0VXN6), Homo sapiens (O95932), Homo sapiens (P00488), Homo sapiens (P21980), Homo sapiens (P22735), Homo sapiens (Q08188), Mus musculus (P21981)
Manually annotated by BRENDA team
Katt, W.P.; Antonyak, M.A.; Cerione, R.A.
Opening up about tissue transglutaminase when conformation matters more than enzymatic activity
Med One
3
e180011
2018
Homo sapiens (P21980)
Manually annotated by BRENDA team
Ha, H.J.; Kwon, S.; Jeong, E.M.; Kim, C.M.; Lee, K.B.; Kim, I.G.; Park, H.H.
Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity
PLoS ONE
13
e0204707
2018
Homo sapiens (P21980), Homo sapiens
Manually annotated by BRENDA team