Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase

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

EC NUMBER
COMMENTARY
2.3.2.13
-
RECOMMENDED NAME
GeneOntology No.
protein-glutamine gamma-glutamyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
mechanism and structure; modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
putative incorporation site of putrescine in beta-casein
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
liver transglutaminase, Q155 and Q159 are putative sites in bovine beta-lactoglobulin that incorporate putrescine
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
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
show the reaction diagram
mechanism, Ca2+ binding in both sites two and three cooperate in opening a channel through the enzyme
Q08188
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
mechanism of regulation by guanine nucleotides and Ca2+/Mg2+, GTPase cycle
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
model for binding and reaction of small peptide substrates, via Michaelis-complex
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
BmTGA
-
-
chloroplast transglutaminase
-
-
chlTGase
-
-
factor XIII
-
-
factor XIIIa
-
-
-
-
fibrin stabilizing factor
-
-
-
-
fibrinoligase
-
-
-
-
glutamine:amine gamma-glutamyl-transferase
-
-
glutaminylpeptide gamma-glutamyltransferase
-
-
-
-
glutamyltransferase, glutaminylpeptide gamma-
-
-
-
-
Laki-Lorand factor
-
-
microbial transglutaminase
-
-
MTG
Streptomyces mobaraensis s-8112
-
-
-
polyamine transglutaminase
-
-
-
-
protein-glutamine gamma-glutamyltransferase
-
-
protein-glutamine gamma-glutamyltransferase
Streptomyces mobaraensis s-8112
-
-
-
R-glutaminyl-peptide:amine gamma-glutamyl transferase
-
-
-
-
STG I
Q6YNC7
-
TG2
Q7M0F8
-
TG2
P21980
-
TG4
Q8BZH1
-
TGase
-
-
TGase
P21980
-
TGase
-
-
TGase
Nemipterus sp.
-
-
TGase
-
-
TGase
Q0GYU0
-
TGase
Streptomyces hygroscopicus WSH03-13
-
-
-
TGase
Streptomyces mobaraensis 40847, Streptomyces mobaraensis DSM 40587, Streptomyces mobaraensis s-8112
-
-
-
TGase
-
-
Tgase 3
-
-
TGase2
-
-
TGM2
P21980
-
TGZ
-
-
tissue transglutaminase
-
-
-
-
tissue transglutaminase
Q7M0F8
-
tissue transglutaminase
-
-
tissue transglutaminase
P21980
-
tissue transglutaminase
-
-
tissue transglutaminase
-
-
tissue transglutaminase 2
-
-
tissue transglutaminase 2
P21980
-
transglutaminase
-
-
-
-
transglutaminase
-
-
transglutaminase
-
-
transglutaminase
Streptomyces mobaraensis DSM 40587
-
-
-
transglutaminase
-
-
transglutaminase 2
-
-
transglutaminase 2
P21980
-
transglutaminase C
-
-
transglutaminase factor XIII
-
-
transglutaminase-2
-
-
tTG
-
-
tTG-2
-
-
type I transglutaminase
-
-
type-2 transglutaminase
-
-
CAS REGISTRY NUMBER
COMMENTARY
80146-85-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
calf
-
-
Manually annotated by BRENDA team
higher activity in 100% confluent endothelial cells than in 50% confluent cells
-
-
Manually annotated by BRENDA team
adult female parasite, responsible for human lymohatic filariasis
-
-
Manually annotated by BRENDA team
comparison of enzyme expression in normal tissue and spontaneous tumours
-
-
Manually annotated by BRENDA team
cloned in Escherichia coli
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli with His-tag
-
-
Manually annotated by BRENDA team
Hartley strain
-
-
Manually annotated by BRENDA team
Cavia porcellus Hartley
Hartley strain
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
comparison of enzyme expression in normal tissue and spontaneous tumours
-
-
Manually annotated by BRENDA team
coagulation factor XIIIa
-
-
Manually annotated by BRENDA team
coagulation factor XIIIa; zymogen factor XIII i.e. proenzyme of XIIIa
-
-
Manually annotated by BRENDA team
coeliac patients and healthy indivuduals
-
-
Manually annotated by BRENDA team
commentary
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
expression in baculovirus system
-
-
Manually annotated by BRENDA team
expression in baculovirus sytem
Uniprot
Manually annotated by BRENDA team
expression in Nicotiana tabacum cultured cells
-
-
Manually annotated by BRENDA team
expression in SK-n-BE(2) neuroblastoma cell
-
-
Manually annotated by BRENDA team
factor XIIIa
-
-
Manually annotated by BRENDA team
isoform TG2
-
-
Manually annotated by BRENDA team
isoform TG2
UniProt
Manually annotated by BRENDA team
isoform tTG
-
-
Manually annotated by BRENDA team
patients with deficiencies in enzyme activity
-
-
Manually annotated by BRENDA team
recombinant endothelial enzyme
-
-
Manually annotated by BRENDA team
recombinant factor XIIIa
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
cultivar Golden Delicious
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
BALB/c strain
-
-
Manually annotated by BRENDA team
newborn, CF57 strain
-
-
Manually annotated by BRENDA team
NZB/W F1 mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
BALB/c strain
-
-
Manually annotated by BRENDA team
Mus musculus CF57
newborn, CF57 strain
-
-
Manually annotated by BRENDA team
Nemipterus sp.
-
-
-
Manually annotated by BRENDA team
L. cv. Samsun
-
-
Manually annotated by BRENDA team
Merino sheep
-
-
Manually annotated by BRENDA team
red sea bream
-
-
Manually annotated by BRENDA team
; enzyme has GTPase and ATPase activity
SwissProt
Manually annotated by BRENDA team
isozymes from hemocyte and muscle
-
-
Manually annotated by BRENDA team
isoforms PtTGA, PtTGB
-
-
Manually annotated by BRENDA team
slime mould, strain M3cV
-
-
Manually annotated by BRENDA team
pea, var. Kelvedon wonder
-
-
Manually annotated by BRENDA team
distribution
-
-
Manually annotated by BRENDA team
male Sasco/King (SD)BR strain
-
-
Manually annotated by BRENDA team
male Sprague Dawley rats
-
-
Manually annotated by BRENDA team
mature male Wistar
-
-
Manually annotated by BRENDA team
tissue-type transglutaminase, abbrevation TGC
-
-
Manually annotated by BRENDA team
Rattus norvegicus male Sasco/King (SD)BR
male Sasco/King (SD)BR strain
-
-
Manually annotated by BRENDA team
expression as inclusion bodies in Escherichia coli
-
-
Manually annotated by BRENDA team
Streptomyces hygroscopicus WSH03-13
WSH03-13
-
-
Manually annotated by BRENDA team
; expression in Escherichia coli
-
-
Manually annotated by BRENDA team
commercial product
-
-
Manually annotated by BRENDA team
strain 40847
-
-
Manually annotated by BRENDA team
Streptomyces mobaraensis 40847
strain 40847
-
-
Manually annotated by BRENDA team
Streptomyces mobaraensis DSM 40587
-
-
-
Manually annotated by BRENDA team
Streptomyces mobaraensis s-8112
-
-
-
Manually annotated by BRENDA team
; expression in Streptomyces lividans
-
-
Manually annotated by BRENDA team
tentatively classified, strain S-8112
-
-
Manually annotated by BRENDA team
japanese horseshoe crab
-
-
Manually annotated by BRENDA team
; patent WWO03102128, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
cultivar G-5054
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
transglutaminase 2 (TG2) mutations are associated with diabetes type 2. Lack of TG2 reduces glucose-stimulated insulin secretion from the pancreatic islets
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
Q964D3
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
Q9JLF6
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
-
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
-
the enzyme reduces the pore diameter and inhibits the activity of transient receptor potential vanilloid 5 in an N-glycosylation-dependent manner
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
show the reaction diagram
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
show the reaction diagram
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
10-kDa heat shock protein-bound gamma-glutamine + methylamine
10-kDa heat shock protein N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
2-N-benzoyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + Abeta1-40
?
show the reaction diagram
-
residues 1-40 of beta-amyloid protein
-
-
?
2-N-benzoyloxycarbonyl-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
-
-
-
-
?
Ac-PQLPF-NH2 + putrescine
?
show the reaction diagram
-
-
-
-
?
actin + ?
?
show the reaction diagram
-
-
-
-
?
actin-bound gamma-glutamine + methylamine
actin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
alpha-actin-bound gamma-glutamine + methylamine
alpha-actin N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
alpha-difluoroornithine + casein
?
show the reaction diagram
-
suicide substrate
-
-
?
alpha-lactalbumin + carbobenzoxy-L-glutaminylglycine
?
show the reaction diagram
-
-
-
-
?
alpha-lactalbumin + dansylcadaverine
?
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
-
-
?
apomyoglobin + carbobenzoxy-L-glutaminylglycine
?
show the reaction diagram
-
-
-
-
?
apomyoglobin + dansylcadaverine
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-glutaminglycine + glycine ethyl ester
benzyloxycarbonyl-alpha-L-glutamyl(gamma-glycine ethyl ester)glycine + NH3
show the reaction diagram
-
-
-
r
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
-
-
?
CBP40 + ?
?
show the reaction diagram
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
Cbz-L-Gln-Gly + ?
?
show the reaction diagram
-
-
-
-
-
Cbz-L-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
Cbz-L-Glu(gamma-p-nitrophenyl ester)-Gly + ?
?
show the reaction diagram
-
-
-
-
?
Cbz-L-Glu(gamma-p-nitrophenyl ester)-Gly + ?
?
show the reaction diagram
P08587
-
-
-
-
Cbz-Phe-GABA umbelliferyl ester + ?
?
show the reaction diagram
-
-
-
-
?
chlathrin heavy chain-bound gamma-glutamine + methylamine
clathrin heavy chain N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
dansylcadaverine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
DQMMLPWPAVAL + spermine
?
show the reaction diagram
-
specific substrate of factor XIII
-
-
?
EAQQIVM + monodansylcadaverine
?
show the reaction diagram
-
liver transglutaminase, peptide derived from the N-terminal sequence of fibronection, first modified residue is mainly Q3
-
-
?
exendin 4 + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
modification at residues K12 and K27 of exendin 4
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
show the reaction diagram
-
-
-
-
?
fibronectin-bound gamma-glutamine + 5-biotinamidopentylamine
fibronectin N5-biotinamidopentylglutamine + NH3
show the reaction diagram
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
show the reaction diagram
Q7M0F8
-
-
-
?
filamin A-bound gamma-glutamine + methylamine
filamin A N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
fluorescein-4-isothiocyanate-beta-AQG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
show the reaction diagram
P81453
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 + ?
show the reaction diagram
P81453
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
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-, Q8T316
-
-
-
-
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Mg2+-dependent GTP hydrolytic activity
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
intrinsic GTPase activity
-
?
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
-
-
-
-
?
histamine + acetyl-alphaS1-casein
?
show the reaction diagram
-
-
-
-
?
histamine + maleyl-bovine serum albumin
?
show the reaction diagram
-
-
-
-
?
HQSYVDPWMLDH + spermine
?
show the reaction diagram
-
specific substrate of factor XIII
-
-
?
hydroxylamine + carbobenzoxy-Gln-Gly
carbobenzoxy-Gln-Gly-hydroxamate + ?
show the reaction diagram
-
other substrates are carbobenzoxy-Gln-Gln-Gly, carbobenzoxy-Gly-Gln-Gln-Gly, carbobenzoxy-Gly-Gly-Gln-Gly with 38%, 13% and 28% efficiency, respectively
-
?
leishmanolysin + alkylamine
?
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
-
-
?
methylamine + succinyl-beta-casein
?
show the reaction diagram
-
transglutaminase B
-
-
?
mono-6-amino-6-deoxy-alpha-cyclodextrin + bovine pancreatic trypsin
?
show the reaction diagram
-
-
-
-
?
mono-6-amino-6-deoxy-beta-cyclodextrin + bovine pancreatic trypsin
?
show the reaction diagram
-
-
-
-
?
mono-6-amino-6-deoxy-gamma-cyclodextrin + bovine pancreatic trypsin
?
show the reaction diagram
-
-
-
-
?
monodansylcadaverine + N,N'-dimethylated casein
?
show the reaction diagram
Nemipterus sp.
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
myo-inositol-1-phosphate synthase + alkylamine
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Ala
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Gly-Gly
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Leu
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Phe
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Ser
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Val
?
show the reaction diagram
-
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
show the reaction diagram
-
-
-
-
?
N,N-dimethylcasein + putrescine
?
show the reaction diagram
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
show the reaction diagram
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
show the reaction diagram
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
show the reaction diagram
-
trivial name dansylcadaverine, casein can be replaced by various synthetic peptide acceptors
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
show the reaction diagram
-
trivial name dansylcadaverine
-
-
?
N-(5-aminopentyl)biotinamide + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-glutaminyl-glycine + ovalbumin
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycin + ?
L-glutamic acid-gamma-monohydroxamate + ?
show the reaction diagram
-
specific high-affinity substrate
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
show the reaction diagram
Streptomyces mobaraensis, Streptomyces mobaraensis s-8112
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
show the reaction diagram
Streptomyces hygroscopicus, Streptomyces hygroscopicus WSH03-13
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
show the reaction diagram
Streptomyces mobaraensis, Streptomyces mobaraensis DSM 40587
-
-
-
-
?
N-Cbz-Glu(gamma-p-nitrophenyl ester)Gly + ?
?
show the reaction diagram
-
-
-
-
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
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
-
?
ornithine + casein
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + alanine ethylester
N-acetylalanine ethylester + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl trimethylacetate + H2O
p-nitrophenol + trimethylacetate
show the reaction diagram
-
liver transglutaminase, ester hydrolysis in the presence of Ca2+
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
show the reaction diagram
-
-
-
-
?
pollen cell-wall protein + N',N_-dimethyl casein
?
show the reaction diagram
-
-
-
-
?
PQPQLPYPQPQLPY-NH2 + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
P21980
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
identification of natural protein substrates
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
substrates are membrane-associated erythrocyte proteins
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
substrates are coagulation factor V, alpha2-macroglobulin, platelet myosin, actin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
chondrosarcoma transglutaminase B, no activity with type I collagen and fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
lens transglutaminase, crosslinking of beta-crystallin
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
synthetic peptide acceptors for transglutaminase in descending order: tert-butyloxycarbonylQQIV, tert-butyloxycarbonylAQQIV, pyroglutamic acidQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
synthetic peptide acceptors for factor XIIIa in descending order of affinity: pyroglutamic acidEAQQIV, tert-butyloxycarbonylAQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
crosslinking of Hammersten casein, crosslinking between Ac-IB and Bz-Gly-Lys
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
amine donors: primary amines
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
lens transglutaminase, endogenous substrate beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
recombinant factor XIIIa: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
amine donors: diamines and polyamines
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
substrate fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
substrate carbobenzoxy-L-Gln-Gly
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
transglutaminase B: simultaneously gamma-polymer and alpha-polymer formation
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
liver transglutaminase, amine donors: putrescine, phenylethylamine, glycinamide, histamine, methylamine, ethanolamine, amonia
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
substrates are pepsin, thrombin, cellulase, creatine kinase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
liver transglutaminase: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
no activity with catalase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Mus musculus BALB/c
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + methylamine
protein N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
protein-bound gamma-glutamine + putrescine
?
show the reaction diagram
-
-
-
-
?
putrescine + bovine muscle actin
?
show the reaction diagram
-
preferred substrate
-
-
?
putrescine + casein
?
show the reaction diagram
-
-
-
-
?
putrescine + casein
?
show the reaction diagram
-
-
-
-
?
putrescine + casein
?
show the reaction diagram
-
-
-
-
?
putrescine + casein
?
show the reaction diagram
-
-
-
-
?
putrescine + casein
?
show the reaction diagram
-
alpha- or beta-casein
-
-
?
putrescine + casein
?
show the reaction diagram
-
in vitro acceptor
-
-
?
putrescine + casein
?
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
putrescine + fibronectin
?
show the reaction diagram
-
-
-
-
?
putrescine + fibronectin
?
show the reaction diagram
-
in vivo acceptor
-
-
?
putrescine + L-glutamine
bis-(glutamyl)-putrescine
show the reaction diagram
-
-
-
-
?
putrescine + light-harvesting complex of photosystem II
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
-
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
transglutaminase 5
-
-
-
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermine and spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
Mus musculus CF57
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
show the reaction diagram
Rattus norvegicus male Sasco/King (SD)BR
-
-
-
-
?
putrescine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
putrescine + N,N-dimethylcasein
?
show the reaction diagram
-, Q8T316
-
-
-
?
putrescine-alginate conjugate + dimethylated casein
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
reacion produces edible films with low water vapor permeability and improved mechanical properties
-
?
QLQPFPQPQLPY + 5-biotinamidopentylamine
?
show the reaction diagram
-
-
-
-
?
spectrin alpha-bound gamma-glutamine + methylamine
spectrin alpha N5-methylglutamine + NH3
show the reaction diagram
-
-
-
-
?
spermidine + L-glutamine
bis-(glutamyl)-spermidine
show the reaction diagram
-
-
-
-
?
spermidine + light-harvesting complex of photosystem II
?
show the reaction diagram
-
-
-
-
?
spermidine + N,N-dimethylcasein
?
show the reaction diagram
-
-
-
-
?
spermine + light-harvesting complex of photosystem II
?
show the reaction diagram
-
coupling efficiency in decreasing order: spermine, spermidine, putrescine
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
show the reaction diagram
Streptomyces mobaraensis, Streptomyces mobaraensis 40847
-
TGase mediated biotinylation
-
-
?
sulforhodamine-beta-AQG + NK6-AP
sulforhodamine-labeled NK6-AP + ?
show the reaction diagram
P81453
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
-
SVS I + ?
?
show the reaction diagram
Q8BZH1
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 + ?
?
show the reaction diagram
Q8BZH1
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 + ?
?
show the reaction diagram
Q8BZH1
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
-
?
thermolysin(205-316) + carbobenzoxy-L-glutaminylglycine
?
show the reaction diagram
-
-
-
-
?
thermolysin(205-316) + dansylcadaverine
?
show the reaction diagram
-
-
-
-
?
thylakoid protein + putrescine
?
show the reaction diagram
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
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
-
-
-
-
?
YELQRPYHSELP + biotinylated cadaverine
?
show the reaction diagram
-
preferred substrate, acitve even in the peptide form
-
-
?
YELQRPYHSELP-glutathione-S-transferase + biotinylated cadaverine
?
show the reaction diagram
-
preferred substrate
-
-
?
Z-Gln-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gln-Gly + O-methyl-Gly
?
show the reaction diagram
-
-
-
-
?
monodansylcadaverine + succinylated casein
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
-
additional information
?
-
-
enzyme may be involved in cataractogenesis
-
-
-
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
-
additional information
?
-
-
coupling of mono- and bis-polyamines is catalysed in equal amounts, reaction only occurs in the light
-
-
-
additional information
?
-
-
no substrate: Boc-Gln-Gly
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 0.530 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
?
-
-
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
?
-
-
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
?
-
-
tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
-
-
-
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
?
-
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
?
-
-
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 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
?
-
Q8BZH1
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
-
additional information
?
-
P81453
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
actin + ?
?
show the reaction diagram
-
-
-
-
?
CBP40 + ?
?
show the reaction diagram
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
Cbz-L-Gln-Gly + alkylamine
?
show the reaction diagram
-
-
-
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
show the reaction diagram
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
show the reaction diagram
Q7M0F8
-
-
-
?
myo-inositol-1-phosphate synthase + alkylamine
?
show the reaction diagram
-
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
show the reaction diagram
-
-
-
-
?
N,N-dimethylcasein + putrescine
?
show the reaction diagram
-
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycin + ?
L-glutamic acid-gamma-monohydroxamate + ?
show the reaction diagram
-
specific high-affinity substrate
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
show the reaction diagram
Streptomyces mobaraensis, Streptomyces mobaraensis DSM 40587
-
-
-
-
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
show the reaction diagram
-
-
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
show the reaction diagram
-
-
-
-
?
pollen cell-wall protein + N',N_-dimethyl casein
?
show the reaction diagram
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
-
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Mus musculus BALB/c
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + putrescine
?
show the reaction diagram
-
-
-
-
?
thylakoid protein + putrescine
?
show the reaction diagram
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
leishmanolysin + alkylamine
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
-
additional information
?
-
-
enzyme may be involved in cataractogenesis
-
-
-
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 0.530 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
?
-
-
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
?
-
-
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
?
-
-
tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
activation, can replace Ca2+ to a lesser extent
Ca2+
-
Cys-thiol active binding-site identified; requirement
Ca2+
-
activation of GTPase activity; requirement
Ca2+
-
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+
-
catalytically active monomeric metal-enzyme complex; requirement
Ca2+
-
Ca2+ leads to plasma factor XIIIa dissociation into alpha'- and beta-dimers; catalytically active monomeric metal-enzyme complex; requirement
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+
-
requirement
Ca2+
-
0.5 mM, maximum activity of transglutaminase from coagulating gland; requirement
Ca2+
-
requirement
Ca2+
-
8 mM, approx. 10fold activation; requirement
Ca2+
-
only with N,N'-dimethylcasein as substrate, no activation with plant proteins as substrate; requirement
Ca2+
-
requirement
Ca2+
-
1 mM; mechanism; requirement
Ca2+
-
1 mM; requirement
Ca2+
-
requirement
Ca2+
-
half-maximal activity at 0.7 mM, maximal activity at about 2 mM; requirement
Ca2+
-
brain transglutaminase NI, maximal activity at 0.1 mM, transglutaminase NII, maximal activity at 0.01 mM, inhibition above
Ca2+
-
requirement
Ca2+
-
maximal activity at 10 mM
Ca2+
-
maximal activity at 10 mM Ca2+ in the presence of 700 mM NaCl
Ca2+
Q08188
transglutaminase 3 binds 3 Ca2+ ions, Er3+, Sm3+, Tb3+ and Lu3+ can substitute for Ca2+ to retain activity
Ca2+
-
dependence on, fully activated at 20 mM
Ca2+
-
optimal at 5-10 mM, inhibitory above 10 mM
Ca2+
-, Q8T316
absolute dependence on Ca2+, 50% of activty with 1 mM, 100% activity with 4 mM
Ca2+
-
crystallization data
Ca2+
-, Q6YNC7
required, half-maximal concentration required is 3 mM
Ca2+
-
required, optimal concentration 1.25 mM
Ca2+
Nemipterus sp.
-
enzyme requires Ca2+ up to 1 mM for full activation
Ca2+
-
calcium in the putrescine incorporation assay buffer results in activation of previously latent TG2
Ca2+
-
wild-type binds 6 Ca2+ per monomer. GTPase activity is inhibited by Ca2+
Ca2+
-
optimum activity at 2 mM
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
required
Ca2+
-
required for activity
Ca2+
-
required for catalytic activity
Ca2+
Q7M0F8
dependent on
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
dependent on
Ga3+
-
requirement
Ga3+
-
no activation
KCl
-
about 8fold activation, maximum activation at 0.6-0.8 M
La3+
-
requirement, 0.01-0.1 mM
LiCl
-
about 6fold activation, maximum activation at 0.6-0.8 M
Mg2+
-
stimulation of GTPase activity, 5 mM
Mg2+
-
activation
Mg2+
-
slight activation
Mg2+
-
slight activation
Mg2+
-
required for GTPase activity, but not for GPT binding
Mg2+
-
crystallization data
Mn2+
-
requirement
Mn2+
-
activation, 3.5% as effective as Ca2+
Mn2+
-
slight activation
NaCl
-
about 10fold activation, maximum activation at 0.6-0.8 M
Sr2+
-
activation, 27% as effective as Ca2+
Sr2+
-
slight activation
Sr2+
Nemipterus sp.
-
10 mM Sr2+, activates
Tb3+
-
requirement
Tb3+
-
no activation
Zn2+
-
activation, 24.6% as effective as Ca2+
additional information
-
not activated by trivalenic lanthanide ions, 0.01-0.1 mM
additional information
-
-
additional information
-
not activated by Cu2+
additional information
-
Ca2+ is not required for activity
additional information
-
not activated by Ca2+
additional information
-
not dependent on Ca2+
additional information
-
enzyme is dependent on Ca2+
additional information
-
the enzyme is not affected by Ca2+, Ba2+, K+, or Na+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
(2E)-3-(4-nitrophenyl)-1-(pyridin-3-yl)prop-2-en-1-one
-
reversible, competitive with the acyl donor substrate
(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
-
-
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
-
-
(E)-1-(1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
-
(E)-1-(1-(3-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
-
(E)-1-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
-
(E)-1-(1-(cyclohexylmethyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
-
(E)-1-(1-benzyl-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
-
(NH4)2SO4
Nemipterus sp.
-
-
(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
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-(1-benzothiophen-2-yl)-3-[benzyl(tert-butyl)amino]propan-1-one
-
-
1-(furan-2-yl)-3-[(2-hydroxyethyl)(propan-2-yl)amino]propan-1-one
-
-
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
-
-
2,3-dibromonaphthoquinone
-
0.015 mM, 41.5% inhibition
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-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00025 mM, standard format, at 0.00018 mM, full progress curve
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-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00021 mM, standard format, at 0.00014 mM, full progress curve
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-Aminophenol
-
-
2-Aminothiophenol
-
-
2-bromo-3-hydroxynaphthoquinone
-
0.015 mM, 35.4% inhibition
2-Iodoacetamide
-
-
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 enzymes 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-(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-Aminophenol
-
-
3-aminothiophenol
-
-
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
3-[benzyl(ethyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(propan-2-yl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
-
3-[benzyl(propan-2-yl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(4-nitrophenyl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(thiophen-2-yl)propan-1-one
-
-
3-[bis(2-hydroxyethyl)amino]-1-(furan-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-Aminophenol
-
-
4-aminothiophenol
-
-
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
-
-
-
5,5'-dithiobis (2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mol per mol enzyme, 85% inactivation, not reversed by glutathione
5,5'-dithiobis(2-nitrobenzoic acid)
-
irreversible, carbobenzoxy-Phe protects
5,5'-dithiobis(2-nitrobenzoic acid)
-
reversed by dithiothreitol
5,5'-methanediylbis(1H-indole-2,3-dione)
-
-
5,5'-oxybis(1H-indole-2,3-dione)
-
-
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
-
-
5-hydroxynaphthoquinone
-
0.015 mM, 46.1% inhibition
6,6'-oxybis(1H-indole-2,3-dione)
-
-
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)
ADP
-
complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
alpha-difluoromethylornithine
-
2.6 mM, 50% inhibition of putrescine transfer to casein, suicide substrate, irreversible, competitive to putrescine or fibrinonectin
AMP
-
weak inhibition of liver transglutaminase
ATP
-
3 mM, complete inhibition of rat liver and human brain tissue-type transglutaminase, reversible; 3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
ATP
-
0.5 mM, approx. 60% inhibition of recombinant tranglutaminase
ATP
-
2 mM, 27% inhibition
Ba2+
-
10 mM, complete inhibition
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 [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
irreversible
beta-mercaptoethanolamine
-
mechanism of inhibition, mercapto group significantly influences substrate behaviour
beta-selenoethanolamine
-
-
Boc-DON-Gln-Ile-Val-OMe
-
-
BOC-DON-QIV-OMe
-
0.1 mM and 1 mM for normal skin and keloid scar, respectively
butanolamine
-
-
Ca2+
-
above 10 mM
cadaverine
-
strong, putrescine as substrate
cadaverine
-
2 mM, 70% inhibition
cadaverine
-
complete inhibition at 0.15 mM
Ce3+
-
not reversible by Ca2+
Chlorpromazine
-
reverses calmodulin enzyme stimulation
Co2+
Nemipterus sp.
-
-
CP30a
-
reversible inhibitor
-
CP4d
-
reversible inhibitor
-
CTP
-
3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
Cu2+
-
1 mM, complete inhibition
Cu2+
-
trace amounts, 0.45 mM diethyldithiocarbamate stimulates crude preparation
Cu2+
-
KCN or dithiothreitol restore activity; mechanism
Cu2+
-
strong inactivation
Cu2+
-
10 mM, complete inhibition
Cu2+
-
5 mM CuSO4, 91% inhibition
Cu2+
Nemipterus sp.
-
-
Cu2+
-
strong inhibition
cystamine
-
50% inhibition at 0.022 mM
cystamine
-
2 mM, 58% inhibition
cystamine
-
transglutaminase inhibitor cystamine alleviates the abnormality in liver from NZB/W F1 mice
cystamine
-
significant reduction in TG2 activity in NZB/W F1 mice following cystamine administration
cystamine
-
-
cystamine
-
ameliorates liver fibrosis induced by carbon tetrachloride via inhibition of tissue transglutaminase
cystamine dihydrochloride
-
1 mM and 10 mM for normal skin and keloid scar, respectively
cysteamine
-
50% inhibition at 0.178 mM
cysteine
-
85% inhibition
Dansylcadaverine
-
0.0019 mM, 50% inhibition
diethyl dicarbonate
-
not without Ca2+
dithiothreitol
-
1.5 mM, 42% inhibition, 16.5 mM, 40% inhibition
DMF
-
90% residual activity at 2.5 and 5% (v/v)
EDTA
-
complete inactivation above 10 mM
EDTA
-
5 mM; 5 mM, complete inhibition
EDTA
-
5 mM; reversible
EDTA
-
1 mM, stable in absence of NaCl, inactivation in presence of NaCl
EDTA
-
10 mM, no residual activity
EDTA
-
10 mM, complete inhibition
EDTA
Nemipterus sp.
-
-
EGTA
-
weak, reversible by Ca2+
EGTA
-
2 mM, irreversible
EGTA
-
2.5 mM, 94% inhibition
EGTA
-
5 mM, 100% inhibition
EGTA
-
10 mM, complete inhibition
ERW1041E
-
-
-
ethanolamine
-
-
ethenesulfonic acid (4-bromophenyl)amide
-
-
-
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
-
-
Fe2+
-
-
-
Fe2+
Nemipterus sp.
-
-
-
Fe2+
-
slight inhibition
-
fluorenylmethyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
reversible, competitive with the acyl donor substrate
Gd3+
-
not reversible by Ca2+
GDP
-
inhibits hydrolysis of GTP
GDP
-
at low levels of 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
-
inhibition of tissue transglutaminase
GTP
-
inhibition of tissue transglutaminase
GTP
-
0.1 mM, complete inhibition at suboptimal Ca2+-levels
GTP
-
50% as effective as ATP
GTP
-
0.005 mM, complete inhibition
GTP
-
0.05 mM, 50% inhibition of lens transglutaminase, 0.5 mM, complete inhibition in the presence of 0.5 mM Ca2+, increasing the Ca2+ concentration to 3 mM reverses inhibition
GTP
-
weak inhibition in the millimolar range
GTP
-
0.02-0.1 mM, inhibition of transglutaminases 2 and 3
GTP
-
0.5 mM, almost complete inhibition of recombinant transglutaminase in the presence of 0.5 mM Ca2+, no inhibition in the presence of 2 mM Ca2+
GTP
-
2 mM, 80% inhibition
GTP
-
causes significant shifts in electrophoretic mobility of the protein under native conditions
GTP-gamma-S
-
inhibition of GTP-hydrolysis
GTP-gamma-S
-, Q8T316
1 mM, 60% inhibition of transglutaminase activity in presence of 0.5 mM Ca2+, 0.1 mM, 50% inhibition of GTPase activity
Hg2+
-
5 mM HgCl2, 94% inhibition
HgCl2
-
5 mM, 96% inhibition in the presence of 10 mM Ca2+
histamine
-, Q6YNC7
-
hydroxylamine
-
100 mM, complete inhibition
Hydroxymercuribenzoate
-
99% inactivation
-
indirubin
-
-
-
iodoacetamide
-
0.1 mM, pH 6.8, in the presence of Ca2+, complete inhibition, irreversible, incorporation of 1 mol carbamidomethyl/mol enzyme, substrate protects
iodoacetamide
-
factor XIIIa; not inhibited in the absence of Ca2+, calmodulin regulated transglutaminases is not inhibited
iodoacetamide
-
-
iodoacetamide
-
86% and 91% inhibition of chondrosarcoma transglutaminase B and C respectively
iodoacetamide
-
0.1 mM, pH 6.8, in the presence of Ca2+, complete inhibition, irreversible, incorporation of 1 mol carbamidomethyl/mol enzyme, substrate protects; mechanism
iodoacetamide
-
-
iodoacetamide
-
1 mM, 89% inhibition of DEAE-absorbed transglutaminase
iodoacetamide
-
10 mM, 62% inhibition in the presence of 10 mM Ca2+
iodoacetamide
-, Q6YNC7
-
iodoacetamide
-
0.1 mM and 1 mM for normal skin and keloid scar, respectively
iodoacetic acid
-
10 mM, complete inhibition
isatin
-
weak, reversible inhibitor
isoindigotin
-
-
-
K+
-
1 mM, 41% inhibition
KCC009
-
inhibition of enzyme and subsequent block of fibronectin assembly in the extracellular matrix of glioblastoma cells
KCC009
-
inhibition of enzyme and subsequent block of fibronectin assembly in the extracellular matrix of glioblastoma cells in vitro and in vivo. KCC009 treatment in mice harboring orthotopic glioblastomas sensitizes the tumors to N,N-bis(2-chloroethyl)-N-nitrosourea chemotherapy
KCC009
-
dihydroisoxazole TG2 inhibitor
KCl
-
45% activity at 400 mM
La3+
-
not reversible by Ca2+
LDN-27219
-
reversible, slow-binding inhibitor that appears not to bind at the enzymes active site but rather at the enzymes 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
LDN-27219
-
-
Li+
-
10 mM, complete inhibition
lysine
-
1 mM, 43% inhibition of DEAE-unabsorbed transglutaminase, 90% inhibition of DEAE-absorbed transglutaminase
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-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]benzoate
-
reversible, competitive with the acyl donor substrate
methyl ketone
-
-
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
-
-
Methylamine
-
1.8 mM, 50% inhibition
Mg2+
-
1 mM, complete inhibition
Mg2+
-
slight inhibition
MgCl2
-
5 mM, 88% inhibition, 30% inhibition in the presence of 10 mM Ca2+
Mn2+
Nemipterus sp.
-
-
Mn2+
-
slight inhibition
monodansyl cadaverine
-
-
Monodansylcadaverine
-
-
Monodansylcadaverine
-
partial inhibition above 0.5 mM
Monodansylcadaverine
-
2 mM, 97% inhibition
Monodansylcadaverine
-
-
Monodansylcadaverine
-
-
Monodansylcadaverine
-
-
Monodansylcadaverine
-
inhibition of glutamyl transfer to putrescine-pectin and putrescine-alginate
Monodansylcadaverine
Q9JLF6
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. TGase-1 interacts with Janus-activated kinase JAK2, and this interaction is inhibited by monodansylcadaverine
monoiodoacetate
-
1 mM, 94% inhibition
monoiodoacetate
-
1 mM, 97% inhibition
monoiodoacetate
-
1 mM, 24% inhibition
monoiodoacetate
-
1 mM, 93% inhibition of DEAE-unabsorbed transglutaminase, 85% inhibition of DEAE-absorbed transglutaminase
N-(2-bromophenyl)acrylamide
-
-
-
N-(3-bromophenyl)acrylamide
-
-
-
N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycine
-
irreversible, ratio kinact to Ki 0.33 micromol per min
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-(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-carbobenzyloxy-L-phenylalanine 2-(acrylamido)ethylamide
-
-
N-carbobenzyloxy-L-phenylalanine 4-(acrylamido)butylamide
-
-
N-carbobenzyloxy-L-phenylalanine 4-(chloroacetylamido)butylamide
-
-
N-carbobenzyloxy-L-phenylalanine 6-(acrylamido)hexylamide
-
-
N-carbobenzyloxy-L-phenylalanine 6-(chloroacetylamido)hexylamide
-
-
N-carbobenzyloxy-L-phenylalanine 8-(acrylamido)octylamide
-
-
N-ethylmaleimide
-
3.6 mol per mol enzyme, 91% inhibition in the presence of Ca2+, not inhibited in the absence of Ca2+, substrate protects
N-ethylmaleimide
-
strong inactivation in the presence of Ca2+, not inhibited in the absence of Ca2+
N-ethylmaleimide
-
79% inactivation
N-ethylmaleimide
-
1 mM, 98% inhibition
N-ethylmaleimide
-
1 mM, 75% inhibition
N-ethylmaleimide
-
1 mM, 90% inhibition
N-ethylmaleimide
-
0.1 mM
N-ethylmaleimide
-
0.1 mM, 60% inhibition
N-ethylmaleimide
-
1 mM, complete inhibition of DEAE-unabsorbed transglutaminase, 93% inhibition of DEAE-absorbed transglutaminase
N-ethylmaleimide
-
irreversible inhibition, inhibition increases with increasing Ca2+ concentrations, 50% inhibition at 1 mM Ca2+
N-ethylmaleimide
-
strong inactivation
N-ethylmaleimide
-
5 mM, strong
N-ethylmaleimide
-
10 mM, complete inhibition
N-ethylmaleimide
Nemipterus sp.
-
-
N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
-
0.01 mM, 91% and 92% inhibition of chondrosarcoma transglutaminases B and C respectively
N-phenylacrylamide
-
-
-
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(2S)-4-[(3-methoxy-1,2,4-thiadiazol-5-yl)amino]-2-[(phenoxycarbonyl)amino]butanoyl]glycine
-
irreversible, ratio kinact to Ki 0.71 micromol per min
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-[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]glycine
-
-
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
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-[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-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]acetamide
-
reversible, competitive with the acyl donor substrate
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-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N-{[(5S)-3-bromo-4,5-dihydro-1,2-oxazol-5-yl]methyl}-5-fluoro-Nalpha-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N5-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-ornithylglycine
-
irreversible, ratio kinact to Ki 0.55 micromol per min
N6-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-lysylglycine
-
irreversible, ratio kinact to Ki 0.72 micromol per min
Na+
-
1 mM, 57% inhibition
Na-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluorotryptophanamide
-
-
NaCl
-
above 500 mM
NaCl
-
500 mM, 2 h at 20C in the absence of substrate, 86% inhibition, reversible to some extent by dilution
NaCl
-
500 mM, 58% inhibition
NaCl
Nemipterus sp.
-
1.2 M, 25% inhibition
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
study on pharmacokinetics, pharmacodynamics, and bioavailability
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
-
naphthoquinone
-
0.015 mM, complete inhibition
NC-I052
-
irreversible inhibitor
-
NH4+
-
complete inhibition of coagulating gland transglutaminase with more than 1 mM NH4Cl or 20 mM (NH4)2SO4
NH4+
-
5 mM, 36% inhibition
o-phenanthroline
-
not reversible by Ca2+
ornithine
-
weak, suicide substrate in the presence of casein
p-chloromercuribenzoate
-
reversible by glutathione
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
21% inhibition of chondrosarcoma transglutaminase B
p-chloromercuribenzoate
-
1 mM, 98% inhibition
p-chloromercuribenzoate
-
1 mM, 44% inhibition
p-chloromercuribenzoate
-
0.1 mM
p-chloromercuribenzoate
-
strong inactivation
p-chloromercuribenzoate
-
10 mM, complete inhibition
Pb(CH3COO)2
-
1 mM, 56% inhibition
Pb2+
-
5 mM Pb(CH3COO)2, 80% inhibition
phenyl methyl sulfonyl fluoride
-
10 mM, complete inhibition
propanolamine
-
-
putrescine
-
0.1-0.2 mM, substrate inhibition
-
putrescine
-
2 mM, 75% inhibition
-
putrescine
-
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
-
putrescine
-
-
-
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
-
-
-
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
-
-
R281
Q7M0F8
irreversible inhibitor
-
R283
Q7M0F8
irreversible inhibitor
-
S-nitroso-N-acetylpenicillamine
-
NO-donor, 8-16 mM, almost complete inhibition of transglutaminases 1 and 3, weak inhibition of transglutaminase 3
Sodium citrate
-
above 10 mM, complete inactivation
spermidine
-
0.1-0.2 mM, substrate inhibition
spermidine
-
-
spermidine
-
2 mM, 70% inhibition
spermine
-
0.17 mM, 50% inhibition
spermine
-
0.1-0.2 mM, substrate inhibition
spermine
-
2 mM, 68% inhibition
SQAETYR
-
noncompetitive inhibition
-
SYAETYR
-
noncompetitive inhibition
-
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
-
-
tert-butyl N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycinate
-
irreversible, ratio kinact to Ki 0.78 micromol per min
tert-butyl N6-acryloyl-N2-[(benzyloxy)carbonyl]-L-lysylglycinate
-
-
tert-butyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
reversible, competitive with the acyl donor substrate
tetrathionate
-
inactivation, not reversible by dithiothreitol
UTP
-
50% as effective as ATP
vitamin K1
-
0.015 mM, 10% inhibition
vitamin K2
-
0.015 mM, 75% inhibition
Zn2+
-
1 mM, 89% inhibition
Zn2+
-, Q6YNC7
-
Zn2+
-
10 mM, complete inhibition
Zn2+
-
5 mM ZnSO4, 95% inhibition
Zn2+
-
strong inhibition
ZnCl2
-
5 mM, 97.5% inhibition, 43% inhibition in the presence of 10 mM Ca2+
[(2-[[(benzyloxy)carbonyl]amino]-4-[5-(formylamino)-1,2,4-thiadiazol-3-yl]butanoyl)amino]acetic acid
-
-
[(4-[3-(aminocarbonyl)oxiran-2-yl]-2-[[(benzyloxy)carbonyl]amino]butanoyl)amino]acetic acid
-
-
[(5R,8S)-8-{[(benzyloxy)carbonyl]amino}-5-(methoxycarbonyl)-2,7-dioxo-9-phenylnonyl](dimethyl)sulfonium bromide
-
-
[([3-(aminocarbonyl)oxiran-2-yl][[(benzyloxy)carbonyl]amino]acetyl)amino]acetic acid
-
-
[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
-
-
[[(4E)-6-amino-2-[[(benzyloxy)carbonyl]amino]-6-oxohex-4-enoyl]amino]acetic acid
-
-
[[(5E)-7-amino-2-[[(benzyloxy)carbonyl]amino]-7-oxohept-5-enoyl]amino]acetic acid
-
-
[[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]amino]acetic acid
-
-
Monoiodoacetic acid
Nemipterus sp.
-
-
additional information
-
rapid inactivatin of factor XIIIa by trypsin and thrombin in the absence of metal ions
-
additional information
-
not inhibited by adenosine or adenine
-
additional information
-
not inhibited by mono- and dimethylated dansylcadaverine
-
additional information
-
not inhibited by diisopropylfluorophosphate; not inhibited by PMSF; not inhibited by sulfhydryl-reagents in the absence of Ca2+
-
additional information
-
transglutaminase of coagulating gland, not inhibited by GTP
-
additional information
-
not inhibited by diisopropylfluorophosphate
-
additional information
-
-
-
additional information
-
not inhibited by Ba2+, Co2+, Fe3+, K+, Mg2+, Mn2+, Na+, Ni2+, Sr2+
-
additional information
-
not inhibited by GDP
-
additional information
-
rapid degradation of liver tissue transglutaminase in the presence of micro-calpain, GTP-gamma-S inhibits degradation
-
additional information
-
-
-
additional information
-
transglutaminase 1, not inhibited by GTP
-
additional information
-
not inhibitory: beta-mercaptoethanol
-
additional information
-
inhibitory activity in decreasing order: cystamine, spermidine, spermine, putrescine, cysteamine
-
additional information
-
not inhibitory: Ba2+, Ca2+, Co2+, Cu2+, Fe2+, Fe3+, Mg2+, Mn2+, Na+, phenylmethylsulfonyl fluoride, EDTA
-
additional information
-
enzyme precursor protein is inhibitory to mature enzyme, even after heat treatment. Precursor is secreted to culture medium; heat-treated pro-enzyme acts effectively as inhibitor of mature form
-
additional information
-
not inhibitory: N-carbobenzyloxy-L-phenylalanine 2-(chloroacetylamido)ethylamide
-
additional information
-
not inhibitory: didansylcadaverine
-
additional information
-
the enzyme is not inhibited by ethylenediaminetetraacetic acid, Na+, K+, Ca2+, Mg2+, Ba2+, Mn2+ and Co2+
-
additional information
-
beta-aminoethyl ketones strongly inhibit TGase, alpha- and gamma-aminoalkyl ketones show very weak TGase inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
requirement
dithiothreitol
-
-
dithiothreitol
-
6-8fold activation of lung transglutaminase B, no activation of transglutaminase C
dithiothreitol
-
-
dithiothreitol
-
weak activation
dithiothreitol
-
10 mM, approx. 1.8fold activation
dithiothreitol
-
-
dithiothreitol
-
required for activity of lens transglutaminase
dithiothreitol
-
3.8fold increase in activity at 10 mM
dithiothreitol
-
slight activation at 5 mM
dithiothreitol
-
optimum activity at 10 mM
ethanol
-
enzyme activity is slightly elevated at a lower concentration of ethanol at 25C. With increasing ethanol concentration, the enzyme activity decreases, and in the presence of 50% ethanol the enzyme activity is almost lost after incubation for 30 min at 25C
NaCl
-
700 mM, 15fold activation
Papain
-
limited proteolysis of plasma factor XIII
-
polyinosinic-polycytidylic acid
-
treatment with 15-30 mg/kg polyinosinic-polycytidylic acid results in villous atrophy and activation of TG2 at the villus tips in small intestine
-
reptilase
-
limited proteolysis of plasma factor XIII
-
Thrombin
-
removes blocked NH2-terminal peptide of factor XIII and unmasks reactive thiol-group at Cys-314 to yield catalytically active factor XIIIa, i.e. fibrinoligase, from inactive zymogen XIII
-
Thrombin
-
slight activation
-
Thrombin
-
Ca2+-dependent proteolytical activation, in the presence of fibrin
-
Thrombin
-
Ca2+-dependent proteolytical activation, in the presence of fibrin; removes blocked NH2-terminal peptide of factor XIII and unmasks reactive thiol-group at Cys-314 to yield catalytically active factor XIIIa, i.e. fibrinoligase, from inactive zymogen XIII
-
Thrombin
-
-
-
Thrombin
-
guinea pig epidermal enzyme; particulate enzyme
-
Thrombin
-
activation, of proenzyme
-
Trypsin
-
strong activation of epidermal tranglutaminase in the presence of Ca2+
-
Trypsin
-
3fold activation of epidermal transglutaminase, activation is blocked by trypsin-inhibitors
-
Trypsin
-
-
-
glutathione
-
reduced, 2.7fold increase in activity at 5 mM
additional information
-
25fold increase in activity by heating at 56C in the presence of Ca2+
-
additional information
-
3-16fold increase in activity of 72000 Da epidermal transglutaminase isoform by heating at 56C in the presence of calcium
-
additional information
-
a model for TGase-activating protease inhibitor-regulated TGase activation process is proposed
-
additional information
-
the enzyme is secreted as a pro-enzyme which is activated by the endoprotease TAMEP
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0029
-
acetyl-alphaS1-casein
-
recombinant enzyme
-
0.0032
-
acetyl-alphaS1-casein
-
native enzyme
-
0.007
-
Actin
-
platelet transglutaminase
-
2.1
-
alpha-difluoromethylornithine
-
-
2.1
-
alpha-difluoroornithine
-
suicide substrate
7
-
benzyloxycarbonyl-L-glutaminylglycine
-
-
0.0409
-
beta-casein
-
-
-
66
-
carbobenzoxy-L-glutaminylglycine
-
-
0.006
-
casein
-
plasma factor XII, actin
0.011
-
casein
-
platelet transglutaminase
0.012
-
casein
-
gizzard transglutaminase
1.9
-
CBz-Gln-Ala
-
37C, pH 7.0
3.2
-
CBz-Gln-Gly
-
37C, pH 7.0
9.4
-
CBz-Gln-Gly-Gly
-
37C, pH 7.0
7
-
CBz-Gln-Leu
-
37C, pH 7.0
2.7
-
CBz-Gln-Phe
-
37C, pH 7.0
2.9
-
CBz-Gln-Ser
-
37C, pH 7.0
4.4
-
CBz-Gln-Val
-
37C, pH 7.0
0.0019
-
Dansylcadaverine
-
pH 7.4, 30C
0.0044
-
GTP
-
GTPase activity
0.01
-
GTP
-, Q8T316
pH 7.5, 37C
0.38
-
histamine
-
recombinant enzyme
0.52
-
histamine
-
native enzyme
0.0037
-
involucrin
-
recombinant transglutaminase 5
1.43
-
LGPQSKVIG
-
37C, pH 7.4
0.782
-
LGPQSLVIG
-
37C, pH 7.4
0.0044
-
loricrin
-
recombinant transglutaminase 5
-
0.024
-
Methylamine
-
transglutaminase C
0.051
-
Methylamine
-
chondrosarcoma transglutaminase B
0.061
-
Methylamine
-
factor XIIIa
0.01
-
Monodansylcadaverine
-
pH 7.5, 10C, muscle enzyme
0.013
-
Monodansylcadaverine
-
pH 7.5, 10C, hemocyte enzyme
0.017
-
N,N-dimethylcasein
-
pH 9.0, 37C
-
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 25C
-
0.05469
-
N-carboxybenzoyl-L-glutaminyl-glycine
-
pH 6.0, 37C
40.47
-
N-carboxybenzoyl-L-glutaminylglycine
-
at pH 6.0 and 55C
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 25C
-
0.05
-
N-dimethyled casein
-
-
-
0.0033
-
N-methyl-casein
-
pH 7.4, 30C
-
11.2
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
wild type enzyme, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
-
11.5
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
mutant enzyme C230A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
-
30
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
Km above 0.03 mM, mutant enzyme C370A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C; Km above 0.03 mM, mutant enzyme C371A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
-
52.66
-
Nalpha-benzyloxycarbonyl-L-glutaminylglycine
-
in 250 mM Tris acetate buffer (pH 8.0), at 37C
-
1.28
-
NQENVSPLTLLKLGN
-
37C, pH 7.4
0.208
-
NQENVSPLTLLRLGN
-
37C, pH 7.4
0.459
-
NQEQVSPLTLLKLGN
-
37C, pH 7.4
1.35
-
ornithine
-
-
0.035
-
putrescine
-
pH 9.0, 37C
-
0.04
0.05
putrescine
-
-
-
0.04
0.05
putrescine
-
-
-
0.04
-
putrescine
-
soluble liver transglutaminase
-
0.044
-
putrescine
-
membrane-associated liver transglutaminase
-
0.049
-
putrescine
-
-
-
0.051
-
putrescine
-
retinoic-acid-induced enzyme
-
0.065
-
putrescine
-
retinoic acid induced transglutaminase
-
0.098
0.106
putrescine
-
enzyme induced by 12-O-tetradecanoylphorbol-13-acetate or Ca2+
-
0.11
-
putrescine
-
-
-
0.17
-
putrescine
-
-
-
0.17
-
putrescine
-
brain transglutaminase NII
-
0.203
-
putrescine
-
tissue transglutaminase from endothelial cells
-
0.28
-
putrescine
-
brain transglutaminase NI
-
0.6
-
putrescine
-
-
-
9.63
-
putrescine
-
-
-
0.0077
-
small proline-rich protein 3
-
recombinant transglutaminase 5
-
0.0214
-
spermidine
-
-
0.042
-
spermidine
-
-
0.0317
-
spermine
-
-
0.069
-
spermine
-
-
1.16
-
succinylated casein
-
pH 7.5, 10C, hemocyte enzyme
-
1.27
-
succinylated casein
-
pH 7.5, 10C, muscle enzyme
-
1.8
-
Z-Gln-Gly
-
pH 7.4, 30C
0.034
-
Monodansylcadaverine
-
-
additional information
-
additional information
-
Km of dimethyl casein: 1.3 mg/ml
-
additional information
-
additional information
-
hair follicle and liver enzyme with identical kinetic features
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic mechanism
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic study with various transglutaminases: human factor XIIIa, guinea pig liver TGC, rat chondrosarcoma TGB
-
additional information
-
additional information
-
kinetic studies of membrane-associated and soluble enzyme; Km of N,N'-dimethylcasein: 0.44-0.52 mg/ml; membrane-associated liver transglutaminase, Km for N,N'-dimethylcasein: 0.44 mg/ml, soluble transglutaminase, 0.52 mg/ml
-
additional information
-
additional information
-
kinetic mechanism
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic parameters of wild-type TG2, T360W, and T360A mutants using Ac-PQLPF-NH2 as the acyl-donor and putrescine as the acyl-acceptor
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00035
-
alpha-carbobenzoxy-lysine
-
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N'-N'-dimethylamino-1'naphthalenesulfonyl)diamidopentane as glutamine donor
16.1
-
beta-casein
-
-
-
0.00055
-
Butylamine
-
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane as glutamine donor
51
-
CBz-Gln-Ala
-
37C, pH 7.0
96
-
CBz-Gln-Gly
-
37C, pH 7.0
102
-
CBz-Gln-Gly-Gly
-
37C, pH 7.0
127
-
CBz-Gln-Leu
-
37C, pH 7.0
54
-
CBz-Gln-Phe
-
37C, pH 7.0
66
-
CBz-Gln-Ser
-
37C, pH 7.0
71
-
CBz-Gln-Val
-
37C, pH 7.0
0.00055
-
ethylamine
-
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane as glutamine donor
0.00233
-
involucrin
-
recombinant transglutaminase 5
78
-
LGPQSKVIG
-
37C, pH 7.4
44
-
LGPQSLVIG
-
37C, pH 7.4
0.0035
-
loricrin
-
recombinant transglutaminase 5
-
0.32
-
Methylamine
-
chondrosarcoma transglutaminase B
0.467
-
Methylamine
-
transglutaminase C
0.532
-
N-dimethylated casein
-
-
-
0.17
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
mutant enzyme C230A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
-
0.19
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
wild type enzyme, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
-
35.48
-
Nalpha-benzyloxycarbonyl-L-glutaminylglycine
-
in 250 mM Tris acetate buffer (pH 8.0), at 37C
-
147
-
NQENVSPLTLLKLGN
-
37C, pH 7.4
2.8
-
NQENVSPLTLLRLGN
-
37C, pH 7.4
77.3
-
NQENVSPLTLLRLGN
-
37C, pH 7.4
175
-
NQEQVSPLTLLKLGN
-
37C, pH 7.4
0.0004
-
Propylamine
-
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane as glutamine donor
0.00433
-
small proline-rich protein 3
-
recombinant transglutaminase 5
-
1.86
-
Methylamine
-
factor XIIIa
additional information
-
additional information
-
kinetic parameters of wild-type TG2, T360W, and T360A mutants using Ac-PQLPF-NH2 as the acyl-donor and putrescine as the acyl-acceptor
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00083
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
Km above 0.03 mM, mutant enzyme C371A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
0
0.0055
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
Km above 0.03 mM, mutant enzyme C370A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
0
0.015
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
mutant enzyme C230A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
0
0.017
-
Nalpha-benzyloxycarbonyl-L-Gln-Gly
-
wild type enzyme, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37C
0
0.67
-
Nalpha-benzyloxycarbonyl-L-glutaminylglycine
-
in 250 mM Tris acetate buffer (pH 8.0), at 37C
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.045
-
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.0071
-
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
-
substrate N-methylcasein
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
-
substrate Abeta1-40
0.00018
-
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.041
-
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.0015
-
2-([3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.00014
-
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.019
-
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.00061
-
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.21
-
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
1.04
-
2-Aminophenol
-
pH 8.0, 37C
0.16
-
2-Aminothiophenol
-
pH 8.0, 37C
7.5e-05
-
2-Iodoacetamide
-
-
0.006
-
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
substrate N-methylcasein; transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.5
-
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00025
-
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
substrate N-methylcasein; transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0073
-
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.039
-
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
substrate Abeta1-40; transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.00016
-
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0082
-
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.045
-
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0071
-
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
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
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
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
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
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00017
-
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
-
substrate N-methylcasein; transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.005
-
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
-
substrate Abeta1-40; transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
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
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00018
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.01
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.041
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0015
-
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.18
-
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00014
-
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0042
-
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.019
-
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0011
-
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
-
substrate N-methylcasein; transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
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
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00061
-
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.05
-
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
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
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
1.91
-
3-Aminophenol
-
pH 8.0, 37C
0.16
-
3-aminothiophenol
-
pH 8.0, 37C
1.09
-
4-Aminophenol
-
pH 8.0, 37C
0.63
-
4-aminothiophenol
-
pH 8.0, 37C
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
6e-05
-
Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
-
-
2.28
-
alpha-difluoromethylornithine
-
-
0.0011
-
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
-
substrate N-methylcasein
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
-
substrate Abeta1-40
0.11
-
benzyl [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
pH 9.0, 37C
0.147
-
beta-mercaptoethanolamine
-
pH 8.0, 37C
5.14
-
beta-selenoethanolamine
-
pH 8.0, 37C
0.28
-
butanolamine
-
pH 8.0, 37C
0.004
-
CP30a
-
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25C
-
0.001
-
CP4d
-
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25C
-
2.2
9
ethanolamine
-
pH 8.0, 37C
0.9
-
GTP
-
-
0.041
-
isoindigotin
-
pH and temperature not specified in the publication
-
0.01
-
methyl ketone
-
pH and temperature not specified in the publication
0.014
-
N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycine
-
-
0.009
-
N-carbobenzyloxy-L-phenylalanine 2-(acrylamido)ethylamide
-
-
0.0045
-
N-carbobenzyloxy-L-phenylalanine 4-(acrylamido)butylamide
-
-
0.073
-
N-carbobenzyloxy-L-phenylalanine 4-(chloroacetylamido)butylamide
-
-
0.013
-
N-carbobenzyloxy-L-phenylalanine 6-(acrylamido)hexylamide
-
-
0.006
-
N-carbobenzyloxy-L-phenylalanine 6-(chloroacetylamido)hexylamide
-
-
0.0035
-
N-carbobenzyloxy-L-phenylalanine 8-(acrylamido)octylamide
-
-
0.0013
-
N-[(2S)-4-[(3-methoxy-1,2,4-thiadiazol-5-yl)amino]-2-[(phenoxycarbonyl)amino]butanoyl]glycine
-
-
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, 37C
0.043
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(naphthalen-2-yloxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37C
0.078
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-3-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37C
0.081
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-4-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37C
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, 37C
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, 37C
0.11
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[5-(dimethylamino)naphthalen-2-yl]sulfonyl]-L-tyrosinamide
-
pH 9.0, 37C
0.0011
-
N-[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]glycine
-
-
0.0013
-
N-[[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
0.0023
-
N5-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-ornithylglycine
-
-
0.0017
-
N6-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-lysylglycine
-
-
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
-
pH 9.0, 37C
0.42
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
-
0.019
-
NC-I052
-
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25C
-
2.05
-
propanolamine
-
pH 8.0, 37C
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
-
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
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.09
-
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
-
transpeptidation of 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 by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
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
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.0013
-
tert-butyl N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycinate
-
-
0.014
-
[(2-[[(benzyloxy)carbonyl]amino]-4-[5-(formylamino)-1,2,4-thiadiazol-3-yl]butanoyl)amino]acetic acid
-
-
0.00123
-
[(4-[3-(aminocarbonyl)oxiran-2-yl]-2-[[(benzyloxy)carbonyl]amino]butanoyl)amino]acetic acid
-
-
0.00056
-
[([3-(aminocarbonyl)oxiran-2-yl][[(benzyloxy)carbonyl]amino]acetyl)amino]acetic acid
-
-
0.00275
-
[[(4E)-6-amino-2-[[(benzyloxy)carbonyl]amino]-6-oxohex-4-enoyl]amino]acetic acid
-
-
0.00048
-
[[(5E)-7-amino-2-[[(benzyloxy)carbonyl]amino]-7-oxohept-5-enoyl]amino]acetic acid
-
-
0.00028
-
[[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]amino]acetic acid
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.021
-
(2E)-3-(4-nitrophenyl)-1-(pyridin-3-yl)prop-2-en-1-one
-
pH 7.0, 25
0.0015
-
(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
0.0036
-
(3E)-3-(2-oxopropylidene)-6-(trifluoromethoxy)-1,3-dihydro-2H-indol-2-one
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
0.0028
-
(3E)-4-chloro-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0015
-
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
pH and temperature not specified in the publication
0.0043
-
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
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
-
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
-
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
-
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
-
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
-
pH and temperature not specified in the publication
0.011
-
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
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
-
pH and temperature not specified in the publication
0.0047
-
(3E)-7-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
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
-
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
-
-
0.0069
-
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
-
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 37C
0.0107
-
(E)-1-(1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
25C, pH 7.0
0.0094
-
(E)-1-(1-(3-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
25C, pH 7.0
0.0021
-
(E)-1-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
25C, pH 7.0
0.011
-
(E)-1-(1-(cyclohexylmethyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
25C, pH 7.0
0.0043
-
(E)-1-(1-benzyl-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
P08587
25C, pH 7.0
0.018
-
1,1'-methanediylbis(1H-indole-2,3-dione)
-
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)
-
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)
-
pH and temperature not specified in the publication
0.004
-
1,3-dimethyl-2-[(2-oxopropyl)thio]-1H-imidazol-3-ium
-
-
0.00021
-
1-(1-benzothiophen-2-yl)-3-[benzyl(tert-butyl)amino]propan-1-one
-
pH 7.5
0.00012
-
1-(furan-2-yl)-3-[(2-hydroxyethyl)(propan-2-yl)amino]propan-1-one
-
pH 7.5
2.5e-05
-
1-ethyl-3-(4-methoxyphenyl)-6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
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 37C
0.033
-
1-[(2E)-3-(4-nitrophenyl)prop-2-enoyl]-3H-[1,2,3]triazolo[4,5-b]pyridin-1-ium-3-olate
-
pH 7.0, 25
-
0.005
-
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
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
-
pH and temperature not specified in the publication
0.028
-
3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide
-
pH 7.0, 25C
0.0005
-
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
-
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 37C
-
0.00058
-
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
-
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 37C
-
9.6e-05
-
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
-
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 37C
-
0.00052
-
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
-
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 37C
-
0.024
-
3-[(2E)-3-(3-nitrophenyl)prop-2-enoyl]-1H-benzotriazol-3-ium-1-olate
-
pH 7.0, 25
0.00042
-
3-[benzyl(ethyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
pH 7.5
0.00019
-
3-[benzyl(propan-2-yl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
pH 7.5
0.00023
-
3-[benzyl(propan-2-yl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
pH 7.5
0.00017
-
3-[benzyl(tert-butyl)amino]-1-(4-nitrophenyl)propan-1-one
-
pH 7.5
8.1e-05
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
pH 7.5
0.0001
-
3-[benzyl(tert-butyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
pH 7.5
0.00044
-
3-[benzyl(tert-butyl)amino]-1-(thiophen-2-yl)propan-1-one
-
pH 7.5
0.00036
-
3-[bis(2-hydroxyethyl)amino]-1-(furan-2-yl)propan-1-one
-
pH 7.5
6.9e-05
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
2.6e-05
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00035
-
4-(3-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid benzyl ester
-
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 37C
-
0.00011
-
4-(4-acryloylamino-2-chlorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00019
-
4-(4-acryloylamino-2-fluorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.0025
-
4-(4-acryloylamino-2-methoxybenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00091
-
4-(4-acryloylamino-2-methylbenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00018
-
4-(4-acryloylamino-2-trifluoromethylbenzenesulfonyl)-piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.013
-
4-(4-acryloylamino-3-fluorobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
9.4e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-chlorobenzyl ester
-
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 37C
-
7e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-methylbenzyl ester
-
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 37C
-
0.00011
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-trifluoromethylbenzyl ester
-
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 37C
-
7e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 3,5-difluorobenzyl ester
-
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 37C
-
0.00012
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
4.4e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid cyclopentyl ester
-
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 37C
-
0.00011
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid methyl ester
-
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 37C
-
8.21e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-1-ylmethyl ester
-
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 37C
-
0.00022
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-2-ylmethyl ester
-
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 37C
-
0.0012
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
4.6e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 2,3-difluorobenzyl ester
-
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 37C
-
5.4e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 4-fluorobenzyl ester
-
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 37C
-
7.2e-05
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid ethyl ester
-
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 37C
-
0.00046
-
4-(4-acryloylaminobenzenesulfonyl)[1,4]diazepane-1-carboxylicacid benzyl ester
-
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 37C
-
0.00045
-
4-(4-acryloylaminobenzenesulfonylamino)piperidine-1-carboxylic acid benzyl ester
-
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 37C
-
0.0028
-
4-(4-but-2-enoylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.08
-
4-(4-cyanobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
7.8e-05
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
9.7e-05
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00038
-
4-[(4-acryloylaminobenzenesulfonylamino)methyl]-piperidine-1-carboxylic acid benzyl ester
-
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 37C
-
0.0014
-
4-[4-(1-oxobut-2-ynylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.08
-
4-[4-(2-cyanoacetylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester, 4-[4-(2-ethoxycarbonylvinyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.0023
-
4-[4-(2-fluoroacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.08
-
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
-
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 37C
-
0.0068
-
4-[4-(3-(E)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.00014
-
4-[4-(3-(Z)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.08
-
4-[4-(3-cyanomethylureido)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.016
-
4-[4-(3-diazo-2-oxopropyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.091
-
4-[4-(3-ethoxycarbonylallyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.01
-
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
-
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 37C
-
0.004
-
4-[4-(4-diazo-3-oxobutyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.0045
-
4-[4-(acryloylmethyl-amino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.028
-
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.08
-
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester, 4-[4-(ethoxycarbonylmethylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
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 37C
-
0.076
-
4-[4-acryloylamino-3-(isobutylmethylamino)-benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
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 37C
-
0.03
-
5,5'-methanediylbis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.025
-
5,5'-oxybis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.0003
-
5-(4-acryloylaminobenzenesulfonyl)-2,5-diazabicyclo-[2.2.1]heptane-2-carboxylic acid tert-butyl ester
-
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 37C
-
0.00014
-
5-(4-acryloylaminobenzenesulfonyl)hexahydropyrrolo[3,4-c]pyrrole-2-carboxylic acid benzyl ester
-
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 37C
-
0.03
0.04
6,6'-oxybis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.016
-
ethenesulfonic acid (4-bromophenyl)amide
-
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 37C
-
0.0018
-
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
-
pH and temperature not specified in the publication
0.025
-
fluorenylmethyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
pH 7.0, 25
0.009
-
GTP
-
-
0.1
-
indirubin
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
-
0.008
-
isoindigotin
-
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
-
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
-
pH and temperature not specified in the publication
0.027
-
methyl 4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]benzoate
-
pH 7.0, 25
0.011
-
methyl ketone
-
pH and temperature not specified in the publication
0.005
-
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
-
-
0.08
-
N-(2-bromophenyl)acrylamide
-
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 37C
-
0.003
-
N-(3-bromophenyl)acrylamide
-
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 37C
-
0.043
-
N-(4-bromobenzyl)acrylamide
-
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 37C
-
0.0033
-
N-(4-bromophenyl)acrylamide
-
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 37C
-
0.08
-
N-(4-bromophenyl)propionamide
-
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 37C
-
0.029
-
N-(4-fluorophenyl)acrylamide
-
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 37C
-
0.00013
-
N-(4-[4-[2-(2-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
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 37C
-
5.4e-05
-
N-(4-[4-[2-(3-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
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 37C
-
6e-05
-
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
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 37C
-
0.11
-
N-(phenylcarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.3
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.043
-
N-phenylacrylamide
-
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 37C
-
0.008
-
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.03
-
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.02
-
N-[(benzyloxy)carbonyl]-L-alanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.028
-
N-[(benzyloxy)carbonyl]-L-alpha-aspartyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.35
-
N-[(benzyloxy)carbonyl]-L-isoleucyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.003
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-5-oxo-6-[(1,3,4,5-tetramethyl-1H-imidazol-3-ium-2-yl)sulfanyl]-L-norleucine
-
-
0.02
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(diethylsulfonio)-5-oxo-L-norleucine
-
-
0.01
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.012
-
N-[(benzyloxy)carbonyl]-L-tryptophyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.008
-
N-[(benzyloxy)carbonyl]glycyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
3.2e-05
-
N-[4-(4-cyclopentanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
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 37C
-
0.00011
-
N-[4-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
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 37C
-
0.00018
-
N-[4-(4-phenylpiperazine-1-sulfonyl)phenyl]acrylamide
-
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 37C
-
5.5e-05
-
N-[4-(4-pyridin-2-ylpiperazine-1-sulfonyl)phenyl]acrylamide
-
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 37C
-
0.0057
-
N-[4-(aminomethyl)benzyl]-3-(5-[[[[(E)-2-phenylethenyl]sulfonyl](pyridin-2-ylmethyl)amino]methyl]-1,2,4-oxadiazol-3-yl)benzamide
-
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 37C
0.0013
-
N-[4-(piperazine-1-sulfonyl)phenyl]acrylamide
-
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 37C
-
0.0019
-
N-[4-(pyrrolidine-1-sulfonyl)phenyl]acrylamide
-
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 37C
-
0.005
-
N-[4-methanesulfonylphenyl]acrylamide
-
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 37C
-
0.058
-
N-[4-methoxyphenyl]acrylamide
-
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 37C
-
0.00067
-
N-[4-nitrophenyl]acrylamide
-
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 37C
-
0.026
-
N-[4-phenoxyphenyl]acrylamide
-
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 37C
-
0.045
-
N-[4-toluyl]acrylamide
-
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 37C
-
0.0038
-
N-[4-trifluoromethylphenyl]acrylamide
-
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 37C
-
0.028
-
N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]acetamide
-
pH 7.0, 25
3.4e-05
-
N-[4-[4-(2-phenylcyclopropanecarbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
0.00019
-
N-[4-[4-(2-trifluoromethylphenyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
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 37C
-
2.5e-05
-
N-[4-[4-(3-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
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 37C
-
0.00016
-
N-[4-[4-(3-phenylpropionyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
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 37C
-
0.00038
-
N-[4-[4-(3-phenylpropyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
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 37C
-
5.2e-05
-
N-[4-[4-(3-trifluoromethylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
4.1e-05
-
N-[4-[4-(4,4-difluoropiperidine-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
0.00031
-
N-[4-[4-(4-phenylbutyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
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 37C
-
3.5e-05
-
N-[4-[4-(6-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
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 37C
-
7.6e-05
-
N-[4-[4-(6-trifluoromethylpyridin-3-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
1e-05
-
N-[4-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
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 37C
-
2e-05
-
N-[4-[4-(octahydroisoquinoline-2-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
2.6e-05
-
N-[4-[4-(octahydroquinoline-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
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 37C
-
3.7e-05
-
N-[4-[4-(piperidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
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 37C
-
5.7e-05
-
N-[4-[4-(pyrrolidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
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 37C
-
0.00018
-
N-[5-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-pyridin-2-yl]acrylamide
-
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 37C
-
1.5e-05
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyridin-2-yl]acrylamide
-
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 37C
-
1.4e-05
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyrimidin-2-yl]acrylamide
-
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 37C
-
0.15
-
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
0.03
-
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
-
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 37C
-
0.65
-
SQAETYR
-
in 250 mM Tris acetate buffer (pH 8.0), at 37C
-
0.75
-
SYAETYR
-
in 250 mM Tris acetate buffer (pH 8.0), at 37C
-
0.018
-
tert-butyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
pH 7.0, 25
0.00021
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-ylmethyl]-carbamic acid benzyl ester
-
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 37C
-
0.00022
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-yl]-carbamic acid benzyl ester
-
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 37C
-
0.0015
-
[2-[(4-acryloylaminobenzenesulfonyl)methylamino]ethyl]-methylcarbamic acid benzyl ester
-
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 37C
-
0.0029
-
[4-(4-acryloylpiperazine-1-sulfonyl)phenyl]carbamic acid benzyl ester
-
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 37C
-
0.08
-
[4-[(4-aminophenyl)sulfonyl]piperazin-1-yl](cyclopropyl)methanone
-
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 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00017
-
-
follicle transglutaminase
0.0013
-
-
epidermal transglutaminase
0.0037
-
-
plasma factor XIII
0.0052
-
-
DEAE-unabsorbed transglutaminase
0.0072
-
-
platelet factor XIII
0.01
-
-
recombinant enzyme from lysate supernatant, at pH 7.0 and 25C
0.07
-
-
erythrocyte transglutaminase
0.092
-
-
DEAE-absorbed transglutaminase
0.156
-
-
tissue transglutaminase
0.16
-
-
-
0.33
-
-
purified recombinant enzyme, at pH 7.0 and 25C
0.526
-
-
-
0.546
-
-
-
1.2
-
-
recombinant transglutaminase
2.5
3
-
-
3.92
-
Nemipterus sp.
-
-
8.7
-
-
pH 8.1, 37C, enzyme enzyme expressed in apoplast
8.8
-
-
incorporation of monodansylcadaverine into N,N-dimethylcasein
12.5
-
-
-
17
-
-
pH 7.0, 37C
25
-
-
formation of L-glutamic acid gamma-monohydroxamate
27.2
-
-
wild type enzyme, at pH 6.0 and 37C
27.4
-
-
mutant enzyme N320D, at pH 6.0 and 37C
28.5
-
-
mutant enzyme Y42H, at pH 6.0 and 37C
28.6
-
-
mutant enzyme Y34F/D268N, at pH 6.0 and 37C
28.7
-
-
mutant enzyme N32D/E264D/N320T, at pH 6.0 and 37C
28.9
-
-
mutant enzyme N32D, at pH 6.0 and 37C
29.1
-
-
mutant enzyme V30D, at pH 6.0 and 37C
29.7
-
-
mutant enzyme A10S, at pH 6.0 and 37C
29.8
-
-
mutant enzyme M16T/G283S, at pH 6.0 and 37C
30.1
-
-
mutant enzyme Q74L, at pH 6.0 and 37C
30.2
-
-
mutant enzyme V6T, at pH 6.0 and 37C
30.3
-
-
mutant enzyme R238F, at pH 6.0 and 37C
30.4
-
-
mutant enzyme R26L, at pH 6.0 and 37C
30.5
-
-
mutant enzyme D14N, at pH 6.0 and 37C; mutant enzyme V30T, at pH 6.0 and 37C
30.6
-
-
mutant enzyme S303A, at pH 6.0 and 37C; mutant enzyme S303F, at pH 6.0 and 37C
30.7
-
-
mutant enzyme R238L, at pH 6.0 and 37C
30.9
-
-
mutant enzyme S284T, at pH 6.0 and 37C
31.4
-
-
mutant enzyme T77L, at pH 6.0 and 37C
31.6
-
-
mutant enzyme Y75H, at pH 6.0 and 37C
32.1
-
-
mutant enzyme S299L, at pH 6.0 and 37C
32.3
-
-
mutant enzyme E28D, at pH 6.0 and 37C; mutant enzyme P12S, at pH 6.0 and 37C
32.4
-
-
mutant enzyme D3L, at pH 6.0 and 37C; mutant enzyme S303T, at pH 6.0 and 37C
32.7
-
-
mutant enzyme E58D, at pH 6.0 and 37C
33
-
-
mutant enzyme H289Y, at pH 6.0 and 37C
33.4
-
-
mutant enzyme R5K, at pH 6.0 and 37C
33.5
-
-
mutant enzyme D3N, at pH 6.0 and 37C
33.6
-
-
mutant enzyme T77A, at pH 6.0 and 37C
33.8
-
-
mutant enzyme V30I, at pH 6.0 and 37C
34.1
-
-
mutant enzyme T77F, at pH 6.0 and 37C
34.3
-
-
mutant enzyme Y34F, at pH 6.0 and 37C
34.4
-
-
mutant enzyme Q74N, at pH 6.0 and 37C
34.9
-
-
mutant enzyme H289F, at pH 6.0 and 37C
35.5
-
-
mutant enzyme R26F, at pH 6.0 and 37C; mutant enzyme Y75A, at pH 6.0 and 37C
35.8
-
-
mutant enzyme D3F, at pH 6.0 and 37C
35.9
-
-
mutant enzyme W59F, at pH 6.0 and 37C
36
-
-
mutant enzyme V65I, at pH 6.0 and 37C
36.6
-
-
mutant enzyme T77S, at pH 6.0 and 37C
37.4
-
-
mutant enzyme Q74A, at pH 6.0 and 37C
41.7
-
-
mutant enzyme Y75F, at pH 6.0 and 37C
42.5
-
-
mutant enzyme M16T, at pH 6.0 and 37C
42.9
-
-
mutant enzyme S199A , at pH 6.0 and 37C
91.7
-
-
pH 8.1, 37C, enzyme expressed in chloroplast
197
-
-
pH 7.5, 37C
additional information
-
-
938 amine incorporation units/min
additional information
-
-
catalytic properties of recombinant liver transglutaminase differ from tat of the native enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7
-
hydroxamate formation from N-carboxybenzoyl-L-glutaminyl-glycine and hydroxylamine
6
-
-
approx. value, hydrolysis reaction
7.5
-
-
less than 50% of maximal activity at pH 5,5 and pH 9.5
7.6
-
-
-
8
-
-
-
8.5
9
-
-
8.5
9
Nemipterus sp.
-
-
9.5
-
-
-
10
-
-
-
additional information
-
-
pI: 5.6
additional information
-
-
pI: 7.6, crude enzyme; pI: 8.5-8.7, purified enzyme
additional information
-
-
-
additional information
-
-
pI: 8.9
additional information
-
-
pI: 6.1
additional information
-
-
optima depend on amine donor substrate
additional information
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
pH 5.0: about 80% of maximal activity, pH 8.0: about 80% of maximal activity
6.5
10
Nemipterus sp.
-
pH 6.5: about 65% of maximal activity, pH 10.0: about 60% of maximal activity
8.3
9.5
-
transamidating activity of guinea pig TG2 was not significantly inhibited at pH 8.3 but minimal at pH 9.5
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
-
-
43% of maximum activity, hemocyte enzyme
5
-
-
60% of maximum activity, hemocyte enzyme
15
-
-
hemocyte enzyme
20
-
-
-
25
-
-
assay at
30
-
-
assay at
35
-
-
assay at
35
-
-
assay at
37
45
-
at pH 6.0, hydroxamate formation from N-carboxybenzoyl-L-glutaminyl-glycine and hydroxylamine
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
-
50
-
-
at pH 6.0
50
-
Nemipterus sp.
-
-
60
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
50
-
at pH 6.0, 30C: about 70% of maximal activity, 50C: about 70% of maximal activity
35
40
-
muscle enzyme
40
60
Nemipterus sp.
-
40C: about 50% of maximal activity, 60C: about 90% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.56
-
-
calculated
5.8
-
-, Q0GYS4
calculated
6.53
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
epidermal carcinoma cell line
Manually annotated by BRENDA team
-
lung cancer cell line
Manually annotated by BRENDA team
-
lung cancer cell line A549. After mechanical damage, TGase 2 appears to contribute to membrane resealing
Manually annotated by BRENDA team
-
prominent expression and activity of isoform TGase II
Manually annotated by BRENDA team
-
comparable activity in both promastigote and amastigote
Manually annotated by BRENDA team
-
insulin-like growth factor-I, epidermal growth factor, and insulin markedly increase TG-2 expression and activity. This effect is reduced when glial cultures are primed with both dexamethasone and estradiol. The regulation of TG-2 in astrocytes is signal- and hormone dependent
Manually annotated by BRENDA team
-
prominent expression and activity of isoform TGase II
Manually annotated by BRENDA team
-
identical with enzyme from placenta or platelets
Manually annotated by BRENDA team
-
coagulation factor XIIIa
Manually annotated by BRENDA team
-
identical with enzyme from plasma; placenta
Manually annotated by BRENDA team
-
coagulation factor XIIIa
Manually annotated by BRENDA team
-
placenta; uterus, macrophages
Manually annotated by BRENDA team
-
enhanced serum immunoreactivity to tTG-2 antigens in some patients with multiple myeloma
Manually annotated by BRENDA team
-
brain specific transglutaminases NI and NII
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
-
malignant, swarm chondrosarcoma
Manually annotated by BRENDA team
-
secretion, not immunologically related to tissue-type enzyme or blood factor XIIIa
Manually annotated by BRENDA team
-
muscularis mucosae
Manually annotated by BRENDA team
-
the enzyme is secreted into the apical medium of polarized cultures of rabbit connecting tubule and cortical collecting duct cells
Manually annotated by BRENDA team
-
endogenous TGase activity increases during developmental cell death reaching a maximum soon after the corolla opening. The activity maximum shifts from proximal to distal part, preceding the developmental cell death acropetal pattern
Manually annotated by BRENDA team
-
the enzyme is detected in the apical medium of polarized cultures of rabbit connecting tubule and cortical collecting duct cells
Manually annotated by BRENDA team
Streptomyces hygroscopicus WSH03-13
-
-
-
Manually annotated by BRENDA team
-
3rd trimester of pregnancy
Manually annotated by BRENDA team
-
monocyte-derived, presence of large amounts of TG2 on cell surface
Manually annotated by BRENDA team
-
TGase activity in the basement membrane region
Manually annotated by BRENDA team
-
muscularis mucosae
Manually annotated by BRENDA team
-
aortic cell suspension culture
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 and MCA3A1-cell line, retinoic acid induced enzyme differs from normal epidermal enzyme
Manually annotated by BRENDA team
Mus musculus BALB/c
-
primary and MCA3A1-cell line, retinoic acid induced enzyme differs from normal epidermal enzyme
-
Manually annotated by BRENDA team
-
callus, keratinocytes
Manually annotated by BRENDA team
-
stratum corneum
Manually annotated by BRENDA team
-
2 epidermal transglutaminases; stratum corneum
Manually annotated by BRENDA team
-
subcellular distribution
Manually annotated by BRENDA team
-
2 isoforms: anionic and cationic
Manually annotated by BRENDA team
Mus musculus BALB/c
-
; subcellular distribution
-
Manually annotated by BRENDA team
Mus musculus CF57
-
2 isoforms: anionic and cationic
-
Manually annotated by BRENDA team
-
primary foreskin fibroblast
Manually annotated by BRENDA team
-
smooth muscle
Manually annotated by BRENDA team
-
isoform TG2 activity is eleveated in glioblastomas compared with non-neoplastic brain
Manually annotated by BRENDA team
-
isoform TG2 activity is elevated in glioblastomas compared with non-neoplastic brain
Manually annotated by BRENDA team
Q964D3
mRNA expression and TGase enzyme activity are high in hematopoietic cells, less in the semi-granular hemocyte and very low in the granular cells
Manually annotated by BRENDA team
-
outer root shear cells
Manually annotated by BRENDA team
-
2 cationic isoforms
Manually annotated by BRENDA team
-
not related to liver enzyme
Manually annotated by BRENDA team
Mus musculus CF57
-
2 cationic isoforms
-
Manually annotated by BRENDA team
Q964D3
TGase is one of the most abundant proteins in hematopoietic tissue. mRNA expression and enzyme activity are high in hematopoietic cells, less in the semi-granular hemocyte and very low in the granular cells
Manually annotated by BRENDA team
Q964D3
mRNA expression and TGase enzyme activity are high in hematopoietic cells, less in the semi-granular hemocyte and very low in the granular cells
Manually annotated by BRENDA team
-
lens epithelial cell line
Manually annotated by BRENDA team
-
lens epithelial line. TGFbeta mediates activation of transglutaminase 2 in response to oxidative stress that leads to protein aggregation
Manually annotated by BRENDA team
-
cell line derived from small intestine crypt cells
Manually annotated by BRENDA team
-
leukemia cell line
Manually annotated by BRENDA team
-
transglutaminase 5
Manually annotated by BRENDA team
-
a diurnal trend of TGase activity is observed in plants under natural conditions in the forest, with the highest value corresponding to the maximum light intensity and amount of light received by the leaves. Plants that are in darkness until midday and suddenly exposed to high light intensity show enhanced TGase activity
Manually annotated by BRENDA team
-
in tobacco mosaic virus-inoculated leaves, TGase activity increases from 24 h onwards relative to controls
Manually annotated by BRENDA team
-
prominent expression and activity of isoform TGase II
Manually annotated by BRENDA team
-
in regenerating liver enhanced formation of Gln-Lys bonds catalyzed by TG2 leads to reduced DNA synthesis
Manually annotated by BRENDA team
Nemipterus sp.
-
-
Manually annotated by BRENDA team
-
administration of pinocembrin, one of the major components of propolis, inhibits tTG activation and significantly prevents the development of thioacetamide-induced liver cirrhosis. tTG may be an important member of the cascade of factors necessary for ethanol-induced liver fibrogenesis. Pinocembrin could serve as an anti-fibrogenic agent
Manually annotated by BRENDA team
Cavia porcellus Hartley, Rattus norvegicus male Sasco/King (SD)BR
-
-
-
Manually annotated by BRENDA team
-
monocyte-derived, presence of large amounts of TG2 on cell surface
Manually annotated by BRENDA team
-
no expression of isoform TGase II in normal mammary tissue and that showing benign hyperplasia, but 44% of mammary carcinomas strongly express isoform TGase II in either a stromal, cellular or combined pattern
Manually annotated by BRENDA team
-
no expression of isoform TGase II in normal mammary tissue and that showing benign hyperplasia, but 83% of mammary carcinomas strongly express isoform TGase II in either a stromal, cellular or combined pattern
Manually annotated by BRENDA team
-
breast cancer cell line
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
-
striated adductor muscle
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
-
in the mouse model of coronary ligation, modulation of FXIII activity by therapy impacts myocardial healing
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
-
identical with enzyme from plasma; platelets
Manually annotated by BRENDA team
-
macrophages; platelets
Manually annotated by BRENDA team
-
isoform tTG protein and RNA are present in stromal cells and trophoblasts in first trimester and at term, with higher levels later in pregnancy
Manually annotated by BRENDA team
-
vascular smooth muscle, extracellular TG2 interacts with the low density lipoprotein related protein 5 receptor and activates beta-catenin signaling in VSMCs. These results suggest that TG2 may promote vascular calcification by activating the beta-catenin signaling pathway
Manually annotated by BRENDA team
-
comparable activity in both promastigote and amastigote
Manually annotated by BRENDA team
Q9JLF6
cells express isoform TGase-1, but not TGase-2, -5, and -7
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
-
apical meristematic tissue
Manually annotated by BRENDA team
-
neuroblastoma SH-SY5Y cells
Manually annotated by BRENDA team
-
transglutaminase 1, required for the formation of a cornified envelope in stratified squamous epithelia
Manually annotated by BRENDA team
-
epidermal TGase activity is observed in stratum granulosum
Manually annotated by BRENDA team
-
enzyme activity is most pronounced in the duodenum, and decreased progressively in the jejunum and ileum
Manually annotated by BRENDA team
-
acute poly(I:C) injury results in rapid TG2 activation
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
-
In the self-incompatible styles, the TGase activity is higher in comparison to style pollinated with compatible pollen, and high molecular mass cross-linked products are formed, suggesting an involvement of TGase in self-incompatible pollen response
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
-
presence of TG2 on cell surface in bowel tissue sections from both normal and celiac subjects
Manually annotated by BRENDA team
-
the enzyme is secreted into the pro-urine
Manually annotated by BRENDA team
-
primary cell, extracellular TG2 interacts with the low density lipoprotein related protein 5 receptor and activates beta-catenin signaling in VSMCs. These results suggest that TG2 may promote vascular calcification by activating the beta-catenin signaling pathway
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
TG2 shows an ubiquitous expression pattern of this protein throughout the body
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
relationship between developmental cell death and TGase. TGase possibly released in the cell wall through the Golgi vesicles could cooperate to cell wall strengthening, especially at the abscission zone and possibly during corolla shape change
Manually annotated by BRENDA team
-
prevalent in thylakoid
Manually annotated by BRENDA team
-
positive correlation between enzyme level and activity. Enzyme is mainly localized to pro-thylakoids and appressed grana thylakoids
Manually annotated by BRENDA team
-
tissue transglutaminase, factor XIIIa
Manually annotated by BRENDA team
-
of microplasmodia, isoform PtTGA
Manually annotated by BRENDA team
-
positive correlation between enzyme level and activity
Manually annotated by BRENDA team
-
colocalization of isoform TG2 and fibronectin in glioblastoma extracellular matrix and secretion of high levels of enzyme and fibronectin by small clusters of invading human glioblastoma cells present in non-neoplastic brain
-
Manually annotated by BRENDA team
-
isoform tTG activity is associated with fibroblast extracellular matrix
-
Manually annotated by BRENDA team
-
the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in vivo. Physical or certain types of chemical injury can lead to rapid enzymatic activation
-
Manually annotated by BRENDA team
Q7M0F8
heparin sulfate binding is required for extracellular matrix localization of the enzyme
-
Manually annotated by BRENDA team
Streptomyces mobaraensis 40847
-
-
-
-
Manually annotated by BRENDA team
-
liver transglutaminase, plasma-membrane associated, lateral domain
Manually annotated by BRENDA team
-
transglutaminase 1, membrane-anchored
Manually annotated by BRENDA team
-
outer mitochondrial membrane of cells overexpressing enzyme
Manually annotated by BRENDA team
-
isoform tTG activity is associated with syncytial mircovillus membrane
Manually annotated by BRENDA team
Rattus norvegicus male Sasco/King (SD)BR
-
liver transglutaminase, plasma-membrane associated, lateral domain
-
Manually annotated by BRENDA team
-
on the surface of monocytes and tissue macrophages
-
Manually annotated by BRENDA team
-
tissue transglutaminase of rat hepatocytes
-
Manually annotated by BRENDA team
-
of macroplasmodia, isoform PtTGA
Manually annotated by BRENDA team
-
the plastid TGase, stabilizing the photosystems, could sustain the energy requirements for the senescence progression
Manually annotated by BRENDA team
-
plastid membrane
Manually annotated by BRENDA team
-
depending on state of cell-proliferation, intracellular distribution
-
Manually annotated by BRENDA team
-
retinoic acid induced enzyme
-
Manually annotated by BRENDA team
Cavia porcellus Hartley
-
-
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
retinoic acid induced enzyme
-
-
Manually annotated by BRENDA team
-
outer mitochondrial membrane of cells overexpressing enzyme
Manually annotated by BRENDA team
additional information
-
soluble in cells and organs devoid of significant association with extensive filamentous structure or extracellular matrix, particulate in organs with extensive filamentous structure or extracellular matrix
-
Manually annotated by BRENDA team
additional information
-
expressed in apoplast and chloroplast
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
39500
-
-
gel filtration
40000
-
-
gel filtration
50000
-
-
epidermal and hair follicle cationic isozyme, gel filtration
54000
-
-
hair follicle transglutaminase, gel filtration
55000
-
-
-
55000
-
-
epidermal transglutaminase, gel filtration
55000
-
-
epidermal transglutaminase, gel filtration
55000
-
-
hair follicle transglutaminase, native PAGE
55000
-
-
-
65000
-
-
gel filtration and sucrose density gradient centrifugation
65000
-
-
transglutaminase C, gel filtration
76900
-
-
sedimentation and diffusion
77000
-
-
gel filtration
80000
-
-
gel filtration
80000
-
-
liver transglutaminase, gel filtration
80000
-
-
-
80000
-
-
liver and chondrosarcoma transglutaminase C, gel filtration
80000
-
-
gel filtration
80000
-
-
DEAE-absorbed transglutaminase, gel filtration
82000
-
-
DEAE-unabsorbed transglutaminase, gel filtration
83010
-
-
primary structure
86000
94000
-
sedimentation equilibrium
88000
-
-
tissue transglutaminase, gel filtration
90000
-
-
sedimentation equilibrium, meniscus depletion method, iodoacetamide-incorporation studies
90000
-
-
epidermis anionic isozyme, gel filtration
90000
-
-