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Enzyme Nomenclature
Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase
for references in articles please use BRENDA:EC2.3.2.13
Word Map on EC 2.3.2.13
- 2.3.2.13
- celiac
- coagulation
-
fibrinogen
- clot
-
crosslinking
- thrombin
-
gluten
-
fxiii
-
serological
- autoimmune
- children
- bleeding
- keratinocytes
- platelet
-
gluten-free
- collagen
-
autoantibody
-
gliadin
-
anti-tissue
- fibronectin
- duodenal
-
healing
-
keratin
- bowel
-
fibrinolysis
-
deamidated
-
villous
- involucrin
- plasminogen
-
isopeptide
-
cornified
- enteropathy
-
prothrombin
- ichthyosis
-
hemostatic
-
malabsorption
- plasmin
-
marsh
-
endoscopy
-
texture
-
gelation
-
cryoprecipitate
-
rheological
- histiocytomas
-
fibrinopeptide
-
d-dimers
-
leiden
- cadaverine
- analysis
-
2-antiplasmin
- food industry
- thrombophilias
- synthesis
- biotechnology
- nutrition
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.3.2.13
-
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RECOMMENDED NAME
GeneOntology No.
protein-glutamine gamma-glutamyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure; modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
putative incorporation site of putrescine in beta-casein
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
liver transglutaminase, Q155 and Q159 are putative sites in bovine beta-lactoglobulin that incorporate putrescine
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism, Ca2+ binding in both sites two and three cooperate in opening a channel through the enzyme
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism of regulation by guanine nucleotides and Ca2+/Mg2+, GTPase cycle
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
model for binding and reaction of small peptide substrates, via Michaelis-complex
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
the first step in both types of modifications is the acylation of the active site cysteine (Cys277) of TG2 by a protein-bound glutamine residue, resulting in the liberation of ammonia and the formation of a thioester intermediate between TG2 and the glutamine bearing protein substrate. In TG2 catalyzed transamidation, the thioester intermediate is attacked by a nucleophilic primary amine, either a small molecule amine such as putrescine or the epsilon-amino group of protein-bound lysine residues. This results in the formation of relatively stable isopeptide bonds
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
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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
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CAS REGISTRY NUMBER
COMMENTARY
80146-85-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
comparison of enzyme expression in normal tissue and spontaneous tumours
-
-
8 distinct transglutaminase isoenzymes have been identified on the genomic level, 6 have been isolated and characterized: factor XIII, type 1 or keratinocyte transglutaminase, type 2 or tissue transglutaminase, type 3 or epidermal transglutaminase, type 4 or prostate transglutaminase and type 5 transglutaminase
-
-
higher activity in 100% confluent endothelial cells than in 50% confluent cells
-
-
-
487821, 487822, 487823, 487828, 487830, 487833, 487834, 487835, 487841, 487842, 487845, 487849, 487856, 487858, 487864, 487867, 487869, 487871, 487872, 487877, 657706, 658011, 672570, 674585, 687721, 689380, 702291, 702612, 705301, 718574, 737135
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-
-
487820, 487823, 487824, 487825, 487826, 487827, 487828, 487829, 487830, 487831, 487832, 487835, 487836, 487839, 487845, 487859, 487862, 487867, 487869, 487870, 487875, 487876, 658011, 658871, 672218, 672575, 673022, 676265, 684390, 685610, 685824, 685853, 685934, 685996, 686142, 686486, 686641, 687207, 687247, 688157, 688721, 688921, 689380, 690146, 701672, 703673, 704481, 704599, 704726, 704990, 706018, 718564, 719054, 719171, 719877, 735910, 735930, 736069, 736141, 736618, 737130
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-
enzyme activity is elevated after oxidative stress or UV irradiation. Intrinsic activity or activation of enzyme is cell-type specific and does not correlate with enzyme expression level
-
-
-
487830, 673022, 676265, 684321, 686486, 686579, 686583, 686760, 689380, 689721, 701637, 718563, 718564, 719171, 719249, 720275, 720850, 736082, 736442, 737260
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-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
transglutaminase 2 (TG2) mutations are associated with diabetes type 2. Lack of TG2 reduces glucose-stimulated insulin secretion from the pancreatic islets
malfunction
enzyme inactivation significantly reduces the virulence of Streptococcus suis serotype 2 in a pig infection model and impairs its antiphagocytosis in human blood
physiological function
-
inhibition of TGase activity with monodansylcadervine, or knockdown of TGase-1 with small interference RNA enhances apoptosis and decreased cell survival in hydrogen peroxide-treated renal proximal tubule cells. Overexpression of TGase-1 renders renal proximal tubule cells more resistant to hydrogen peroxide toxicity and monodansylcadaverine treatment blocks this response. Concurrent with renal proximal tubule cells apoptosis, phosphorylation of AKT, signal transducer and activator of transcription-3, and glucogen synthase kinase-3 are observed. Pretreatment of cells with monodansylcadervine or TGase-1 siRNA inhibits phosphorylation of all these molecules
physiological function
complete knock-down by RNAi results in changed cell morphology, and cells start to spread intensely. After addition of astakine, a cytokine involved in hematopoiesis, cells start to spread and adopt a morphology similar to that observed after RNAi of TGase. Astakine has no effect on TGase expression, but after a prolonged incubation for one week, TGase activity inside and outside the cells is completely lost
physiological function
-
presence of bacterial lipopolysaccharide increases the level of TG2 on the surface of maturing dendritic cells
physiological function
-
TG2 regulates the expression and function of matrix metalloproteinase MMP-2. TG2 knockdown down-regulates MMP-2 protein and mRNA expression in SKOV-3, IGROV-1, MDA-MB-436, and PC-3 cancer cells. TG2 knockdown or inhibition of TG2 activity using KCC009 decreases MMP-2 gelatinase activity in cancer cells. MMP-2 expression and function are regulated by TG2 at transcriptional level. Binding of CREB to the MMP-2 promoter is diminished in cells that express decreased TG2 levels. TG2 knockdown decreases CREB phosphorylation, and CREB knockdown decreases MMP-2 expression. The effect of TG2 on CREB activity and MMP-2 transcription is mediated by TG2-dependent degradation of protein phosphatase PP2A-alpha. PP2A-alpha complexes with and is targeted for degradation by TG2
physiological function
treatment of proximal renal tublule cells with inhibitor monodansylcadaverine or siRNA results in decreased proliferation accompanied by activation of signal transducer and activator of transcription, Akt and Stat-3. Treatment with monodansylcadaverine or TGase-1 siRNA decreases Stat-3 but not Akt phosphorylation. Janus-activated kinase JAK2 mediates phosphorylation of Stat-3, and knockdown of either JAK2 or Stat-3 by siRNA decreases cell proliferation. Inhibition of TGase-1 decreases phosphorylation of Stat-3 but not JAK2. JAK2 is indispensable for TGase-1 to induce Stat-3 phosphorylation and TGase-1 potentiates JAK2-induced Stat-3 phosphorylation. Inhibition of TGase-1 and the JAK2-Stat-3 signaling pathway decreases the transcriptional activity of Stat-3 and expression of the Stat-3-targeted genes, cyclin D1 and cyclin E. TGase-1 interacts with JAK2, and this interaction is inhibited by monodansylcadaverine
physiological function
-
TG2 binds to the Rac-binding pocket in the GTPase-activating domains of regulator proteins Bcr and Abr, blocks Bcr activity and, through this mechanism, increases levels of active GTP-bound Rac and EGF-stimulated membraneruffling. Bcr exhibits preferential binding to the non-compacted conformation of TG2, in which its catalytic domain is exposed, but transamidation is not needed for the interaction
physiological function
-
TGase 2 has a role as a biological glue to consolidate various micro-structural components of tissues and biomaterials
physiological function
-
hypoxia induces TG2 expression through an HIF-1 dependent pathway and concurrently activates intracellular TG2. The hypoxiccells overexpressing TG2 show resistance to apoptosis. Hypoxic cells treated with either TG2 inhibitor or small interfering RNA become sensitive to apoptosis. Activation of TG2 in response to hypoxic stress inhibits caspase-3 activity by forming crosslinked multimer, resulting in insoluble aggregates. TG2 also activates nuclear factor kappaB pathway after hypoxic stress, and thereby induces the expression of cellular inhibitor of apoptosis 2
physiological function
-
tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination. The number of melanoma lung foci is more markedly reduced by enzyme overexpression than the metastatic size
physiological function
-
tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination. The number of melanoma lung foci is more markedly reduced by enzyme overexpression than the metastatic size
physiological function
-
the enzyme is involved in the apical growth of apple pollen tube
physiological function
-
phosphorylation of transglutaminase 2 at Ser216 plays a role in transglutaminase 2-mediated activation of nuclear factor-kappaB, Akt and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
physiological function
-
phosphorylation of transglutaminase 2 at Ser216 plays a role in transglutaminase 2-mediated activation of nuclear factor-kappaB, Akt and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
physiological function
-
the enzyme reduces the pore diameter and inhibits the activity of transient receptor potential vanilloid 5 in an N-glycosylation-dependent manner
physiological function
major and functional transglutaminas of Macrobrachium rosenbergii for haemolymph coagulation and also in spread of infection
physiological function
-
transglutaminase 2 is involved in homocysteine-induced activation of human THP-1 monocytes
physiological function
-
the enzyme has an intrinsic capability to promote cell survival and contributes to oncogenesis
physiological function
the enzyme is a virulence factor in Streptococcus suis serotype 2 with antiphagocytic activity
physiological function
-
the enzyme is associated with amyloid-beta deposits and lesion-associated astrocytes in Alzheimer's disease
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
10-kDa heat shock protein-bound gamma-glutamine + methylamine
10-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + Abeta1-40
?
-
residues 1-40 of beta-amyloid protein
-
-
?
60-kDa heat shock protein-bound gamma-glutamine + methylamine
60-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
actin-bound gamma-glutamine + methylamine
actin N5-methylglutamine + NH3
-
-
-
-
?
alpha-actin-bound gamma-glutamine + methylamine
alpha-actin N5-methylglutamine + NH3
-
-
-
-
?
alpha-N-t-butyloxycarbonyl-L-Lys-CH2-CH2-dansyl + N,N-dimethylcasein
?
-
-
-
-
-
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
?
-
i.e. beta-amyloid protein peptide comprising residues 1-40
-
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + N,N-dimethylated casein
?
-
transpeptidation
-
-
?
benzyloxycarbonyl-L-glutaminglycine + glycine ethyl ester
benzyloxycarbonyl-alpha-L-glutamyl(gamma-glycine ethyl ester)glycine + NH3
-
-
-
r
biotinyl-5-pentylamine + N,N'-dimethylcasein
?
-
covalent incorporation of biotinyl-5-pentylamine into N,N'-dimethylcasein
-
-
?
biotinylated TVQQEL + calcium binding protein S100A7
?
-
transglutaminase 2
-
-
?
CBP40 + ?
?
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
chlathrin heavy chain-bound gamma-glutamine + methylamine
clathrin heavy chain N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 1 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 1 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 2 epidermal keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 2 epidermal keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 5 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 5 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 6A keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 6A keratin type II N5-methylglutamine + NH3
-
-
-
-
?
EAQQIVM + monodansylcadaverine
?
-
liver transglutaminase, peptide derived from the N-terminal sequence of fibronection, first modified residue is mainly Q3
-
-
?
exendin 4 + 5-biotinamidopentylamine
?
-
-
modification at residues K12 and K27 of exendin 4
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + 5-biotinamidopentylamine
fibronectin N5-biotinamidopentylglutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
-
-
-
?
filamin A-bound gamma-glutamine + methylamine
filamin A N5-methylglutamine + NH3
-
-
-
-
?
fluorescein-4-isothiocyanate-beta-AQG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
-
fluorescein-4-isothiocyanate-epsilon-aminocaproate-QG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
-
galectin-3-bound gamma-glutamine + methylamine
galectin-3 N5-methylglutamine + NH3
-
-
-
-
?
H2A histone type 1-bound gamma-glutamine + methylamine
H2A histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H2B histone type 1-bound gamma-glutamine + methylamine
H2B histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H4 histone -bound gamma-glutamine + methylamine
H4 histone N5-methylglutamine + NH3
-
-
-
-
?
hydroxylamine + carbobenzoxy-Gln-Gly
carbobenzoxy-Gln-Gly-hydroxamate + ?
-
other substrates are carbobenzoxy-Gln-Gln-Gly, carbobenzoxy-Gly-Gln-Gln-Gly, carbobenzoxy-Gly-Gly-Gln-Gly with 38%, 13% and 28% efficiency, respectively
-
?
LGPQSKVIG + glycine-ethylester
?
-
i.e. K9, an optimized sequence based on beta-casein
-
-
?
LGPQSLVIG + glycine ethylester
?
-
i.e. K9(K7L), a modified optimized sequence based on beta-casein
-
-
?
mono-6-amino-6-deoxy-alpha-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-beta-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-gamma-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
-
specific high-affinity substrate
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
-
-
-
-
?
neuropeptide Y + 5-biotinamidopentylamine
?
-
-
modification at residue Q34 of neuropeptide Y
-
?
NNEQVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q2N
-
-
?
NQENVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N
-
-
?
NQENVSPLTLLLLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12L
-
-
?
NQENVSPLTLLRLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12R
-
-
?
nucleophosmin-bound gamma-glutamine + methylamine
nucleophosmin N5-methylglutamine + NH3
-
-
-
-
?
orexin B + 5-biotinamidopentylamine
?
-
-
modification at residues Q8 and Q12 of orexin B
-
?
p-nitrophenyl acetate + alanine ethylester
N-acetylalanine ethylester + p-nitrophenol
-
-
-
?
p-nitrophenyl trimethylacetate + H2O
p-nitrophenol + trimethylacetate
-
liver transglutaminase, ester hydrolysis in the presence of Ca2+
-
?
plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
-
preferred substrate
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
-
-
-
-
?
protein-bound gamma-glutamine + methylamine
protein N5-methylglutamine + NH3
-
-
-
-
?
putrescine-alginate conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + soy flour protein
?
-
-
reacion produces edible films with low water vapor permeability and improved mechanical properties
-
?
spectrin alpha-bound gamma-glutamine + methylamine
spectrin alpha N5-methylglutamine + NH3
-
-
-
-
?
spermine + light-harvesting complex of photosystem II
?
-
coupling efficiency in decreasing order: spermine, spermidine, putrescine
-
-
?
sulforhodamine-beta-AQG + NK6-AP
sulforhodamine-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
-
SVS I + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS II + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS III + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
thylakoid protein + putrescine
?
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
vimentin-bound gamma-glutamine + methylamine
vimentin N5-methylglutamine + NH3
-
-
-
-
?
YELQRPYHSELP + biotinylated cadaverine
?
-
preferred substrate, acitve even in the peptide form
-
-
?
YELQRPYHSELP-glutathione-S-transferase + biotinylated cadaverine
?
-
preferred substrate
-
-
?
Z-Gln-Gly + hydroxamate
L-glutamic acid gamma-monohydroxamate + NH3
-
high activity
-
-
?
Z-Gln-Gly + Nalpha-acetyl-L-lysine methyl ester
?
-
high activity
-
-
?
Z-Gln-Gly + propargylamine
Z-Nepsilon-propargyl-Gln-Gly + NH3
-
high activity
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[casein]-L-glutamine + alkylamine
[casein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[casein]-L-glutamine + biotin-labeled pentylamine
? + NH3
-
-
-
?
[T26 protein]-L-glutamine + 5-(biotinamido)-pentylamine
[T26 protein]-N5-pentyl-L-glutamine + biotin
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
GTP + H2O
GDP + phosphate
-
Mg2+-dependent GTP hydrolytic activity
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
trivial name dansylcadaverine, casein can be replaced by various synthetic peptide acceptors
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, endogenous substrate beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate carbobenzoxy-L-Gln-Gly
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase, amine donors: putrescine, phenylethylamine, glycinamide, histamine, methylamine, ethanolamine, amonia
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transaminase catalyzes also the hydrolysis and aminolysis of certain aliphatic amides and of active and some inactive esters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with benzyloxycarbonyl-L-glutaminylglycine, benzyloxycarbonyl-alpha-L-glutamyl(gamma-p-nitrophenyl ester) glycine, guinea pig hair follicle enzyme
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are acetylated B-chains of oxidized insulin
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of recombinant full-length transglutaminase 5: loricrin, small proline rich proteins 1, 2 and 3, and involucrin
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are membrane-associated erythrocyte proteins
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are coagulation factor V, alpha2-macroglobulin, platelet myosin, actin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of transglutaminase I and II: EF-hand-containing calcium binding proteins S100A11, S100A10 and S100A07
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for factor XIIIa in descending order of affinity: pyroglutamic acidEAQQIV, tert-butyloxycarbonylAQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: primary amines
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
recombinant factor XIIIa: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitior to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
endogenous substrates: cellular proteins e.g. aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphorylase kinase, crystallins, gluthathione S-transferase, actin, myosin, troponin, beta-tubulin, tau, Rho A, histone, alpha-oxoglutarate dehydrogenase, cytochromes, erythrocyte band III, CD38, acetylcholine esterase, collagen, fibronectin, fibrinogen, vitronectin, osteopontin, nidogen, laminin, LTBP-1, osteonectin, osteocalcin, substance P, phospholipase A2, midkine, exogenous substrates: wheat gliadin, whey proteins, soy proteins, pea legumin, Candida albicans surface proteins, HIV envelope glycoproteins gp120 and gp41, HIV aspartyl proteinase, hepatitis C virus core protein
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, crosslinking of beta-crystallin
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for transglutaminase in descending order: tert-butyloxycarbonylQQIV, tert-butyloxycarbonylAQQIV, pyroglutamic acidQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
crosslinking of Hammersten casein, crosslinking between Ac-IB and Bz-Gly-Lys
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: diamines and polyamines
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are pepsin, thrombin, cellulase, creatine kinase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with catalase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
chondrosarcoma transglutaminase B, no activity with type I collagen and fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase B: simultaneously gamma-polymer and alpha-polymer formation
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with bovine myosin, histone mixture, human serum fibronectin, spinach ribulose 1,5-diphosphate carboxylase-oxygenase, carbobenzoxyglutamine, carbobenzoxy-Asn-Gly
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
identification of natural protein substrates
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine and spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
additional information
?
-
-
screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like Q-nonconserved amino acid-P-hydrophobic amino acid-D(P), Q-nonconserved amino acid-P-hydrophobic amino acid, or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-DP
-
-
-
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5–30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
-
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Bothamyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase-induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
-
additional information
?
-
-
enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
-
-
-
additional information
?
-
-
enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
-
-
-
additional information
?
-
-
surface tissue transglutaminase amplifies integrin-mediated signaling to RhoA/Rho-associated coiled-coil containing serine/threonine protein kinase ROCK via integrin clustering and down.regulation of the Src-p190RhoGAP regulatory pathway
-
-
-
additional information
?
-
-
screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-WP
-
-
-
additional information
?
-
-
study of enzyme specificity with Q-containing substrates based on beta-casein, K9-peptide and alpha2-antiplasmin. Factor XIIIa preferentially selects the Q2 residue for carrying out crosslinking processes.The E3 and Q4 provide supporting role in binding. When reaction occurs at Q2, then Q4 is sterically blocked. Deamidation of Q2 to E2 allows observation of reactivity at Q4. K12 position provides an additional favorable site of interaction with factor XIIIa surface
-
-
-
additional information
?
-
-
functions of TG2: wound healing, macrophage phagocytosis, TGF-beta activation, protein kinase activity, association with calreticulin, and association with G-protein coupled receptor GPR56. The majority of these functions are independent of the enzymatic transamidation activity of the protein. Transglutaminase 2 is involved in the pathogenesis of a number of diseases, such as celiac sprue, neurodegenerative disorders, diabetes, liver cirrhosis and fibrosis, renal scarring, and certain types of cancer. It is the enzymatic function of TG2 that is thought to contribute to the pathology or etiology of most of the aforementioned diseases
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
-
additional information
?
-
-
transglutaminase catalyses the crosslinking of proteins by formation of an isopeptide bond between a glutamyl carboxamide in one protein and a lysyl epsilon-amino group of another protein
-
-
-
additional information
?
-
-
type I transglutaminase catalyzes the formation of epsilon-(gamma-glutamyl)lysine bonds and is the key protein responsible for generation of the crosslinks. Tazarotene-induced gene 3 (TIG3) regulates TG1 activity
-
-
-
additional information
?
-
-
vimentin is a major arterial substrate for transglutaminase, transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated
-
-
-
additional information
?
-
-
enzyme preferably uses those glutamine and lysine residues that are in intrinsically disordered regions. To explain the complex physicochemical interaction between TG2 and its substrates spatial features must be considered as well
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
-
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
-
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
-
additional information
?
-
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
-
additional information
?
-
-
the enzyme uses pepT26-bound gamma-glutamine, vimentin-bound gamma-glutamine, actin-bound gamma-glutamine, heat shock protein 71-bound gamma-glutamine, heat shock protein 90-bound gamma-glutamine, beta-actin-like protein 2-bound gamma-glutamine, serpin H1-bound gamma-glutamine, heat shock protein 60-bound gamma-glutamine, lysozyme C1-bound gamma-glutamine, endoplasmin-bound gamma-glutamine, collagen alpha-1(III) chain-bound gamma-glutamine, elongation factor 1-alpha1-bound gamma-glutamine as substrates
-
-
-
additional information
?
-
Nemipterus sp.
-
enzyme catalyzes the cross-linking of the myosin heavy chains of Nemipterus sp.
-
-
-
additional information
?
-
-
possible role of TGase activity in the defense against a viral plant pathogen
-
-
-
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
-
additional information
?
-
-
transglutaminase reactions function in response to mechanical injury. Among the substrates are actin, 40 kDa Ca2+-binding protein CBP40, and a 33 kDa protein highly homologous to the eukaryotic adenine nucleotide translocator
-
-
-
additional information
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
-
additional information
?
-
-
TG2 is related to cell growth at an early stage of liver regeneration after partial hepatectomy, and regulates the growth capacity through down-regulation of the EGF receptor
-
-
-
additional information
?
-
MTG can accept diverse fluorophores such asdansyl, fluorescein, and rhodamine derivatives in place of the benzyloxycarbonyl moiety when linked via a beta-alanine or epsilon-aminocaproic acid linker
-
-
-
additional information
?
-
-
posttranslational dimerization and multimerization of Camelidae anti-human TNF single domain antibodies in vitro catalyzed by microbial transglutaminases. Ribonuclease S-tag-peptide acts as a peptidyl substrate in covalent protein cross-linking reactions catalyzed by MTG. C-terminally fusion of the S-tag sequence to the anti-hTNF-variable heavy chain-domain results in fusion proteins that are efficiently dimerized and multimerized by MTG whereas anti-hTNF-variable heavy chain domain is not susceptible to protein crosslinking
-
-
-
additional information
?
-
-
no activity with carbamic acid, thiamine, 2-bromoethylamine, N-ethylmethylamine, sarcosine, butanol, butanethiol, or L-isoleucine methyl ester
-
-
-
additional information
?
-
-
tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CBP40 + ?
?
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
Q7M0F8
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
-
specific high-affinity substrate
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
-
-
-
-
?
plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
-
preferred substrate
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
-
-
-
-
?
thylakoid protein + putrescine
?
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitior to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
A0A024GWU1
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
A0A0S3Q197, A0A0S3Q1B1
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
D9J009
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
D9J009
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
Q2VI01
-
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5–30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
-
additional information
?
-
-
enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
-
-
-
additional information
?
-
-
enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
-
-
-
additional information
?
-
-
surface tissue transglutaminase amplifies integrin-mediated signaling to RhoA/Rho-associated coiled-coil containing serine/threonine protein kinase ROCK via integrin clustering and down.regulation of the Src-p190RhoGAP regulatory pathway
-
-
-
additional information
?
-
-
functions of TG2: wound healing, macrophage phagocytosis, TGF-beta activation, protein kinase activity, association with calreticulin, and association with G-protein coupled receptor GPR56. The majority of these functions are independent of the enzymatic transamidation activity of the protein. Transglutaminase 2 is involved in the pathogenesis of a number of diseases, such as celiac sprue, neurodegenerative disorders, diabetes, liver cirrhosis and fibrosis, renal scarring, and certain types of cancer. It is the enzymatic function of TG2 that is thought to contribute to the pathology or etiology of most of the aforementioned diseases
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
-
additional information
?
-
-
transglutaminase catalyses the crosslinking of proteins by formation of an isopeptide bond between a glutamyl carboxamide in one protein and a lysyl epsilon-amino group of another protein
-
-
-
additional information
?
-
-
type I transglutaminase catalyzes the formation of epsilon-(gamma-glutamyl)lysine bonds and is the key protein responsible for generation of the crosslinks. Tazarotene-induced gene 3 (TIG3) regulates TG1 activity
-
-
-
additional information
?
-
-
vimentin is a major arterial substrate for transglutaminase, transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
-
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
-
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
-
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
-
additional information
?
-
-
transglutaminase reactions function in response to mechanical injury. Among the substrates are actin, 40 kDa Ca2+-binding protein CBP40, and a 33 kDa protein highly homologous to the eukaryotic adenine nucleotide translocator
-
-
-
additional information
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
-
additional information
?
-
-
TG2 is related to cell growth at an early stage of liver regeneration after partial hepatectomy, and regulates the growth capacity through down-regulation of the EGF receptor
-
-
-
additional information
?
-
-
tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ga3+
Mg2+
Mn2+
Sr2+
Tb3+
additional information
Ca2+
-
no activity below 1.25 mM, maximal activity at 2.5 mM and above, half-maximal activity at approx. 1.5 mM; requirement
Ca2+
-
crucial during thrombin cleavage of factor XIII for the formation of factor XIIIa and factor XIIIa activation, Ln3+ can replace Ca2+ during trypsin activation of factor XIII but not in activation of factor XIIIa; requirement
Ca2+
-
Ca2+ leads to plasma factor XIIIa dissociation into alpha'- and beta-dimers; catalytically active monomeric metal-enzyme complex; requirement
Ca2+
-
requirement
Ca2+
transglutaminase 3 binds 3 Ca2+ ions, Er3+, Sm3+, Tb3+ and Lu3+ can substitute for Ca2+ to retain activity
Ca2+
-
calcium in the putrescine incorporation assay buffer results in activation of previously latent TG2
Ca2+
absolute dependence on Ca2+, 50% of activty with 1 mM, 100% activity with 4 mM
Ca2+
-
half-maximal activity at 0.7 mM, maximal activity at about 2 mM; requirement
Ca2+
-
only with N,N'-dimethylcasein as substrate, no activation with plant proteins as substrate; requirement
Ca2+
-
0.5 mM, maximum activity of transglutaminase from coagulating gland; requirement
Ca2+
-
brain transglutaminase NI, maximal activity at 0.1 mM, transglutaminase NII, maximal activity at 0.01 mM, inhibition above
additional information
-
not activated by trivalenic lanthanide ions, 0.01-0.1 mM
additional information
-
the enzyme is not affected by Ca2+, Ba2+, K+, or Na+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1Z)-2-{[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl}ethanehydrazonic acid
-
-
(2-[[(1R)-3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-1-carboxy-3-oxopropyl]amino]-2-oxoethyl)(dimethyl)sulfanium bromide
-
-
(2-[[6-(methoxycarbonyl)naphthalen-2-yl]methoxy]-2-oxoethyl)(dimethyl)sulfonium
-
-
(2E)-3-(4-nitrophenyl)-1-(pyridin-3-yl)prop-2-en-1-one
-
reversible, competitive with the acyl donor substrate
(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-(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)-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-(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-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)-7-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-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
-
-
(E)-1-(1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(3-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(cyclohexylmethyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-benzyl-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(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)-2-(1-(dimethylamino)naphthalene-5-sulfonamido)-3-(1H-indol-3-yl)propanamide
-
the majority of cellular TG2 cannot be inhibited in intact cells. The inhibitor potently inhibits cell lysate TG2 activity in the presence of calcium
(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
-
-
1,3-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-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
-
-
1-[(2E)-3-(4-nitrophenyl)prop-2-enoyl]-3H-[1,2,3]triazolo[4,5-b]pyridin-1-ium-3-olate
-
reversible, competitive with the acyl donor substrate
-
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
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-[(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-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-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide
-
reversible inhibitor and photolabel. In labeling experiments, specific labeling of residue C230
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
-
-
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
-
-
3-[(2E)-3-(3-nitrophenyl)prop-2-enoyl]-1H-benzotriazol-3-ium-1-olate
-
reversible, competitive with the acyl donor substrate
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
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl 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 cyclopenty