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Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase
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2.3.2.13 protein-glutamine gamma-glutamyltransferaseIUBMB Comments
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
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Word Map
- 2.3.2.13
- celiac
- coagulation
- clot
- fibrinogen
-
crosslinking
-
serological
- gluten
- bleeding
- thrombin
- children
- autoimmune
- platelet
- keratinocytes
- autoantibody
- collagen
-
gluten-free
- gliadin
-
anti-tissue
- duodenal
- igg
-
deamidated
- fibronectin
- bowel
-
villous
- plasminogen
-
fibrinolysis
- keratin
-
cornified
- involucrin
-
isopeptide
- enteropathy
- prothrombin
-
hemostatic
-
gelation
- plasmin
-
endoscopy
-
texture
-
marsh
-
gastroenterology
- filaggrin
-
cryoprecipitate
- ichthyosis
-
malabsorption
- leiden
- cadaverine
-
fibrinopeptide
- agriculture
-
2-antiplasmin
- histiocytomas
-
antifibrinolytic
-
sealant
- synthesis
- nutrition
- food industry
- biotechnology
- diagnostics
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AcTG-1, BmTGA, chloroplast transglutaminase, chlTGase, cold active transglutaminase, cold-active transglutaminase, EPB42, factor XIII, factor XIIIa, fibrin stabilizing factor, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
factor XIIIa
KALB
KalbTG
KALB_7456
mammalian transglutaminase
microbial transglutaminase
microbial transglutaminases
MTG
MTG-TX
MTGase
protein-glutamine gamma-glutamyltransferase
SCTG
SMTG
TG-2
TG1
TG2
TG3
TG4
TG5
TG6
TGase
TGase 1
TGase 2
Tgase 3
Tgase II
TGase-2
TGL
TGM1
TGM2
tissue transglutaminase
tissue transglutaminase 2
transglutaminase
transglutaminase 1
transglutaminase 2
transglutaminase 3
transglutaminase 6
transglutaminase factor XIII
tTG
microbial transglutaminase
-
MTG
-
TG2
-
-
TG2
-
transglutaminase 2
-
-
transglutaminase 2
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
ping-pong mechanism
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
liver transglutaminase, Q155 and Q159 are putative sites in bovine beta-lactoglobulin that incorporate putrescine
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
putative incorporation site of putrescine in beta-casein
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism of regulation by guanine nucleotides and Ca2+/Mg2+, GTPase cycle
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism, Ca2+ binding in both sites two and three cooperate in opening a channel through the enzyme
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
model for binding and reaction of small peptide substrates, via Michaelis-complex
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
the first step in both types of modifications is the acylation of the active site cysteine (Cys277) of TG2 by a protein-bound glutamine residue, resulting in the liberation of ammonia and the formation of a thioester intermediate between TG2 and the glutamine bearing protein substrate. In TG2 catalyzed transamidation, the thioester intermediate is attacked by a nucleophilic primary amine, either a small molecule amine such as putrescine or the epsilon-amino group of protein-bound lysine residues. This results in the formation of relatively stable isopeptide bonds
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
the catalytic reaction follows a modified ping-pong mechanism in which a glutamine-containing protein or peptide, the acyl-donor substrate, reacts with the catalytic cysteine residue to form a thioester bond. The resulting covalent acyl-enzyme intermediate then reacts with a second substrate, the acyl-acceptor, to yield the isopeptide-containing product and free enzyme in a transamidation reaction. Substrate specificity of the enzyme, detailed overview
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
ping-pong mechanism
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
protein-glutamine:amine gamma-glutamyltransferase
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
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CAS REGISTRY NUMBER
COMMENTARY
80146-85-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
10-kDa heat shock protein-bound gamma-glutamine + methylamine
10-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + Abeta1-40
?
-
residues 1-40 of beta-amyloid protein
-
-
?
60-kDa heat shock protein-bound gamma-glutamine + methylamine
60-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
actin-bound gamma-glutamine + methylamine
actin N5-methylglutamine + NH3
-
-
-
-
?
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
-
-
-
?
alpha-actin-bound gamma-glutamine + methylamine
alpha-actin N5-methylglutamine + NH3
-
-
-
-
?
alpha-casein glutamine + alkylamine
alpha-casein N5-alkylglutamine + NH3
-
-
-
?
alpha-N-t-butyloxycarbonyl-L-Lys-CH2-CH2-dansyl + N,N-dimethylcasein
?
-
-
-
-
?
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
-
-
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val
?
-
i.e. beta-amyloid protein peptide comprising residues 1-40
-
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + N,N-dimethylated casein
?
-
transpeptidation
-
-
?
benzyloxycarbonyl-L-glutaminglycine + glycine ethyl ester
benzyloxycarbonyl-alpha-L-glutamyl(gamma-glycine ethyl ester)glycine + NH3
-
-
-
r
beta-casein glutamine + hydroxylamine
beta-casein N5-hydroxylglutamine + NH3
-
-
-
?
biotinyl-5-pentylamine + N,N'-dimethylcasein
?
-
covalent incorporation of biotinyl-5-pentylamine into N,N'-dimethylcasein
-
-
?
biotinylated TVQQEL + calcium binding protein S100A7
?
-
transglutaminase 2
-
-
?
bovine serum albumin glutamine + alkylamine
bovine serum albumin N5-alkylglutamine + NH3
-
-
-
-
?
CBP40 + ?
?
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
CBZ-Gln-Gly-OH + hydroxylamine
CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
CBZ-Gly-GABA-coumarin-7-yl ester + hydroxylamine
7-hydroxycoumarin + ?
-
-
-
?
CBZ-Phe-GABA-coumarin-7-yl ester + hydroxylamine
7-hydroxycoumarin + ?
-
-
-
?
clathrin heavy chain-bound gamma-glutamine + methylamine
clathrin heavy chain N5-methylglutamine + NH3
-
-
-
-
?
cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
cornifin-A is SPR1
-
-
?
cytoskeletal 1 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 1 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 2 epidermal keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 2 epidermal keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 5 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 5 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 6A keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 6A keratin type II N5-methylglutamine + NH3
-
-
-
-
?
desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
-
-
-
?
EAQQIVM + monodansylcadaverine
?
-
liver transglutaminase, peptide derived from the N-terminal sequence of fibronection, first modified residue is mainly Q3
-
-
?
epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
-
-
-
?
exendin 4 + 5-biotinamidopentylamine
?
-
-
modification at residues K12 and K27 of exendin 4
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + 5-biotinamidopentylamine
fibronectin N5-biotinamidopentylglutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
-
-
-
?
filamin A-bound gamma-glutamine + methylamine
filamin A N5-methylglutamine + NH3
-
-
-
-
?
fluorescein-4-isothiocyanate-beta-AQG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
fluorescein-4-isothiocyanate-epsilon-aminocaproate-QG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
galectin-3-bound gamma-glutamine + methylamine
galectin-3 N5-methylglutamine + NH3
-
-
-
-
?
H2A histone type 1-bound gamma-glutamine + methylamine
H2A histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H2B histone type 1-bound gamma-glutamine + methylamine
H2B histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H4 histone -bound gamma-glutamine + methylamine
H4 histone N5-methylglutamine + NH3
-
-
-
-
?
hydroxylamine + carbobenzoxy-Gln-Gly
carbobenzoxy-Gln-Gly-hydroxamate + ?
-
other substrates are carbobenzoxy-Gln-Gln-Gly, carbobenzoxy-Gly-Gln-Gln-Gly, carbobenzoxy-Gly-Gly-Gln-Gly with 38%, 13% and 28% efficiency, respectively
-
?
involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
-
-
-
?
junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
-
-
-
?
kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
-
-
-
?
LGPQSKVIG + glycine-ethylester
?
-
i.e. K9, an optimized sequence based on beta-casein
-
-
?
LGPQSLVIG + glycine ethylester
?
-
i.e. K9(K7L), a modified optimized sequence based on beta-casein
-
-
?
mono-6-amino-6-deoxy-alpha-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-beta-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-gamma-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
N,N'-dimethyl casein glutamine + biotinylated pentylamine
?
the enzymatic activity is determined by measuring the fluorescence of biotinylated pentylamine crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
-
specific high-affinity substrate
-
-
?
N-Cbz-Glu(gamma-4-nitrophenylester)Gly + alkylamine
4-nitrophenol + ?
-
-
-
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
-
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
-
-
-
-
?
neuropeptide Y + 5-biotinamidopentylamine
?
-
-
modification at residue Q34 of neuropeptide Y
-
?
NNEQVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q2N
-
-
?
NQENVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N
-
-
?
NQENVSPLTLLLLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12L
-
-
?
NQENVSPLTLLRLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12R
-
-
?
nucleophosmin-bound gamma-glutamine + methylamine
nucleophosmin N5-methylglutamine + NH3
-
-
-
-
?
orexin B + 5-biotinamidopentylamine
?
-
-
modification at residues Q8 and Q12 of orexin B
-
?
p-nitrophenyl acetate + alanine ethylester
N-acetylalanine ethylester + p-nitrophenol
-
-
-
?
p-nitrophenyl trimethylacetate + H2O
p-nitrophenol + trimethylacetate
-
liver transglutaminase, ester hydrolysis in the presence of Ca2+
-
?
plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
-
-
-
?
plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
-
preferred substrate
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
-
-
-
-
?
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + methylamine
protein N5-methylglutamine + NH3
-
-
-
-
?
putrescine-alginate conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + soy flour protein
?
-
-
reacion produces edible films with low water vapor permeability and improved mechanical properties
-
?
spectrin alpha-bound gamma-glutamine + methylamine
spectrin alpha N5-methylglutamine + NH3
-
-
-
-
?
spermine + light-harvesting complex of photosystem II
?
-
coupling efficiency in decreasing order: spermine, spermidine, putrescine
-
-
?
sulforhodamine-beta-AQG + NK6-AP
sulforhodamine-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
SVS I + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS II + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS III + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
thylakoid protein + putrescine
?
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
-
-
-
?
vimentin-bound gamma-glutamine + methylamine
vimentin N5-methylglutamine + NH3
-
-
-
-
?
YELQRPYHSELP + biotinylated cadaverine
?
-
preferred substrate, acitve even in the peptide form
-
-
?
YELQRPYHSELP-glutathione-S-transferase + biotinylated cadaverine
?
-
preferred substrate
-
-
?
YENHKLPSSWPF + alkylamine
Y-N5-alkylglutaminyl-NHKLPSSWPF + NH3
N-terminally biotinylated peptide substrate
-
-
?
YEQHKLPSSWPF + pentylamine
Y-N5-pentylglutaminyl-QHKLPSSWPF + NH3
N-terminally biotinylated peptide substrate
-
-
?
Z-Gln-Gly + hydroxamate
L-glutamic acid gamma-monohydroxamate + NH3
-
high activity
-
-
?
Z-Gln-Gly + hydroxylamine
Z-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Z-Gln-Gly + Nalpha-acetyl-L-lysine methyl ester
?
-
high activity
-
-
?
Z-Gln-Gly + propargylamine
Z-Nepsilon-propargyl-Gln-Gly + NH3
-
high activity
-
-
?
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + alkylamine
Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxy-4-methylcoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + H2O
Z-Phe-gamma-Abu-OH + 7-hydroxy-4-methylcoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxycoumarin + alkylamine
Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxycoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxycoumarin + H2O
Z-Phe-gamma-Abu-OH + 7-hydroxycoumarin
-
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[casein]-L-glutamine + alkylamine
[casein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[casein]-L-glutamine + biotin-labeled pentylamine
? + NH3
-
-
-
?
[T26 protein]-L-glutamine + 5-(biotinamido)-pentylamine
[T26 protein]-N5-pentyl-L-glutamine + biotin
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
-
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
beta-crystallin, a major structural protein of the eye lens, is an archetypal TG2 substrate. Its target Gln residue is localized to a peptide sequence denoted A25 (TVQQEL), and is crosslinked to a Lys residue near the C-terminus of the same protein
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
a TG2 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
a TG2 isozyme specific biotinylated peptide substrate
-
-
?
casein glutamine + pentylamine
casein N5-pentylglutamine + NH3
the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure
-
-
?
casein glutamine + pentylamine
casein N5-pentylglutamine + NH3
the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
Streptomyces cinnamoneus NBRC 13864
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
Streptomyces cinnamoneus NBRC 13864
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
Streptomyces cinnamoneus NBRC 13864
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
the 220 kDa fibronectin monomer harbors multiple Gln residues susceptible to TG2 modification, including sites within its N-terminal collagen/fibrinbinding domain, its central (RGD-containing) integrin-binding domain, and its C-terminal glycosaminoglycan-binding domain. In addition, its N-terminal domain also harbors a high-affinity non-covalent docking site for TG2
-
-
?
GTP + H2O
GDP + phosphate
-
Mg2+-dependent GTP hydrolytic activity
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
-
the enzymatic activity is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein (DMC) exposure. Fluorescence intensity of MDC incorporated into DMC is measured at excitation and emission wavelengths of 350 and 480 nm, respectively
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
the enzymatic activity of AcTG-1 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
the enzymatic activity of TG2 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
trivial name dansylcadaverine, casein can be replaced by various synthetic peptide acceptors
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
Streptomyces cinnamoneus NBRC 13864
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, endogenous substrate beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate carbobenzoxy-L-Gln-Gly
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase, amine donors: putrescine, phenylethylamine, glycinamide, histamine, methylamine, ethanolamine, amonia
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transaminase catalyzes also the hydrolysis and aminolysis of certain aliphatic amides and of active and some inactive esters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with benzyloxycarbonyl-L-glutaminylglycine, benzyloxycarbonyl-alpha-L-glutamyl(gamma-p-nitrophenyl ester) glycine, guinea pig hair follicle enzyme
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are acetylated B-chains of oxidized insulin
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of recombinant full-length transglutaminase 5: loricrin, small proline rich proteins 1, 2 and 3, and involucrin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are membrane-associated erythrocyte proteins
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are coagulation factor V, alpha2-macroglobulin, platelet myosin, actin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of transglutaminase I and II: EF-hand-containing calcium binding proteins S100A11, S100A10 and S100A07
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for factor XIIIa in descending order of affinity: pyroglutamic acidEAQQIV, tert-butyloxycarbonylAQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: primary amines
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
recombinant factor XIIIa: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitior to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
endogenous substrates: cellular proteins e.g. aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphorylase kinase, crystallins, gluthathione S-transferase, actin, myosin, troponin, beta-tubulin, tau, Rho A, histone, alpha-oxoglutarate dehydrogenase, cytochromes, erythrocyte band III, CD38, acetylcholine esterase, collagen, fibronectin, fibrinogen, vitronectin, osteopontin, nidogen, laminin, LTBP-1, osteonectin, osteocalcin, substance P, phospholipase A2, midkine, exogenous substrates: wheat gliadin, whey proteins, soy proteins, pea legumin, Candida albicans surface proteins, HIV envelope glycoproteins gp120 and gp41, HIV aspartyl proteinase, hepatitis C virus core protein
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, crosslinking of beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for transglutaminase in descending order: tert-butyloxycarbonylQQIV, tert-butyloxycarbonylAQQIV, pyroglutamic acidQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
crosslinking of Hammersten casein, crosslinking between Ac-IB and Bz-Gly-Lys
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: diamines and polyamines
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are pepsin, thrombin, cellulase, creatine kinase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with catalase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
chondrosarcoma transglutaminase B, no activity with type I collagen and fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase B: simultaneously gamma-polymer and alpha-polymer formation
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with bovine myosin, histone mixture, human serum fibronectin, spinach ribulose 1,5-diphosphate carboxylase-oxygenase, carbobenzoxyglutamine, carbobenzoxy-Asn-Gly
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
identification of natural protein substrates
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine and spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
additional information
?
-
-
screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like Q-nonconserved amino acid-P-hydrophobic amino acid-D(P), Q-nonconserved amino acid-P-hydrophobic amino acid, or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-DP
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5–30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Bothamyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase-induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
synthesis and kinetic characterisation of water-soluble fluorogenic acyl donors for transglutaminase 2, overview. Development of a fluorimetric TGase 2 activity assay with release of 7-hydroxycoumarin (HC) by TGase 2-catalysed hydrolysis or aminolysis of Z-Phe-gamma-Abu-HC resulting in a measureable increase in fluorescence. No activity with Z-Phe-gamma-Abu-7-amido-4-methylcoumarin and Z-Glu(AMC)-Gly-OH. Because the assay of TGase 2 requires the presence of an antioxidant to prevent oxidation of the active-site cysteine residue, both DTT and tris(2-carboxyethyl)phosphine (TCEP) are employed for investigations into the spontaneous reactivity of the compounds at a concentration of 0.5 mM. C-terminal extension with glycine results in kobs values that are increased by a factor of approximately four
-
-
-
additional information
?
-
wild-type TG2 can catalyze synthesis of CBZ-protected dipeptides. Its donor substrate specificity is narrow, aromatic ester derivatives of Gly and D-Ala serve as donor substrates. A hydrophobic cavity formed by Trp332 and Phe334 dictates substrate specificity. TG2 enzymes exhibit broad specificity towards the acyl-acceptor substrate. Guinea pig liver transglutaminase (gTG2) catalyzes the cross-linking of peptides and proteins via the formation of gamma-glutamyl-epsilon-lysyl isopeptide bonds. gTG2-catalyzed peptide bond formation between various amino acid-derived donor and acceptor substrates is analyzed. gTG2 forms Gly-Xaa and D-Ala-Gly dipeptide products, confirming that the enzyme's natural transamidation activity can be co-opted for peptide synthesis, LC-MS analysis. An aromatic ester of Gly is the most efficient acyl-donor substrate tested, aromatic esters of D-Ala and L-Ala show 50fold lower reactivity or no reactivity, respectively. The native acyl-acceptor substrate is generally a lysine-containing protein or peptide, many nonnatural primary amines, such as glycinamide, and anilines, such as N,N-dimethyl-1,4-phenylenediamine, can also react. TG2 displays narrow specificity for its acyl-donor substrates. The side chain of a protein or peptide-bound L-Gln residue is the native substrate while the side chain of the similar amino acid L-Asn is not reactive. In addition to amides, gamma-glutamyl aromatic ester derivatives of L-Glu, such as Ncarbobenzyloxy-L-glutamyl(gamma-p-nitrophenyl ester)glycine, have also been shown to be acyl-donor substrates of TG2 and are used to measure the enzyme's activity. N-Carbobenzyloxyglycyl-coumarin-7-yl ester (CBZ-Gly-7HC), is also a donor substrate of TG2. Construction of acyl-enzyme intermediates, structure analysis, and structural basis, overview
-
-
-
additional information
?
-
the recombinant transglutaminase crosslinks casein, collagen and gelatin
-
-
-
additional information
?
-
-
the recombinant transglutaminase crosslinks casein, collagen and gelatin
-
-
-
additional information
?
-
-
enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
-
-
?
additional information
?
-
-
enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
-
-
?
additional information
?
-
-
surface tissue transglutaminase amplifies integrin-mediated signaling to RhoA/Rho-associated coiled-coil containing serine/threonine protein kinase ROCK via integrin clustering and down.regulation of the Src-p190RhoGAP regulatory pathway
-
-
?
additional information
?
-
-
screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-WP
-
-
?
additional information
?
-
-
study of enzyme specificity with Q-containing substrates based on beta-casein, K9-peptide and alpha2-antiplasmin. Factor XIIIa preferentially selects the Q2 residue for carrying out crosslinking processes.The E3 and Q4 provide supporting role in binding. When reaction occurs at Q2, then Q4 is sterically blocked. Deamidation of Q2 to E2 allows observation of reactivity at Q4. K12 position provides an additional favorable site of interaction with factor XIIIa surface
-
-
?
additional information
?
-
-
functions of TG2: wound healing, macrophage phagocytosis, TGF-beta activation, protein kinase activity, association with calreticulin, and association with G-protein coupled receptor GPR56. The majority of these functions are independent of the enzymatic transamidation activity of the protein. Transglutaminase 2 is involved in the pathogenesis of a number of diseases, such as celiac sprue, neurodegenerative disorders, diabetes, liver cirrhosis and fibrosis, renal scarring, and certain types of cancer. It is the enzymatic function of TG2 that is thought to contribute to the pathology or etiology of most of the aforementioned diseases
-
-
?
additional information
?
-
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
-
transglutaminase catalyses the crosslinking of proteins by formation of an isopeptide bond between a glutamyl carboxamide in one protein and a lysyl epsilon-amino group of another protein
-
-
?
additional information
?
-
-
type I transglutaminase catalyzes the formation of epsilon-(gamma-glutamyl)lysine bonds and is the key protein responsible for generation of the crosslinks. Tazarotene-induced gene 3 (TIG3) regulates TG1 activity
-
-
?
additional information
?
-
-
vimentin is a major arterial substrate for transglutaminase, transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated
-
-
?
additional information
?
-
-
enzyme preferably uses those glutamine and lysine residues that are in intrinsically disordered regions. To explain the complex physicochemical interaction between TG2 and its substrates spatial features must be considered as well
-
-
?
additional information
?
-
certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
-
-
-
additional information
?
-
-
certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
-
-
-
additional information
?
-
several substrate candidates of TG1 that may be essential for cornified envelope formation are identified and characterized
-
-
-
additional information
?
-
enzyme transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. It is also known to harbor other enzymatic properties, including protein disulfide isomerase, GTP-dependent signal transduction, and ATP dependent protein kinase activity
-
-
-
additional information
?
-
-
enzyme transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. It is also known to harbor other enzymatic properties, including protein disulfide isomerase, GTP-dependent signal transduction, and ATP dependent protein kinase activity
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
-
protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
-
-
-
additional information
?
-
significant differences in the 15(V/K) KIEs on NH3 release determined for the deamidation (0.2%) and the transamidation (2.3%) of Z-Gln-Gly suggest the rate-limiting steps of TG2 active site acylation are dependent on the presence of the acyl acceptor. Substrate-induced conformational changes may play a role in promoting catalysis, mechanism, overview
-
-
-
additional information
?
-
microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
-
-
-
additional information
?
-
-
microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
-
-
-
additional information
?
-
microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
?
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
?
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
?
additional information
?
-
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
?
additional information
?
-
-
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
?
additional information
?
-
-
the enzyme uses pepT26-bound gamma-glutamine, vimentin-bound gamma-glutamine, actin-bound gamma-glutamine, heat shock protein 71-bound gamma-glutamine, heat shock protein 90-bound gamma-glutamine, beta-actin-like protein 2-bound gamma-glutamine, serpin H1-bound gamma-glutamine, heat shock protein 60-bound gamma-glutamine, lysozyme C1-bound gamma-glutamine, endoplasmin-bound gamma-glutamine, collagen alpha-1(III) chain-bound gamma-glutamine, elongation factor 1-alpha1-bound gamma-glutamine as substrates
-
-
?
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
-
the formation of intermolecular cross-links of casein and bovine serum albumin polymerized by MsTGase in the presence of DTT is observed
-
-
-
additional information
?
-
Nemipterus sp.
-
enzyme catalyzes the cross-linking of the myosin heavy chains of Nemipterus sp.
-
-
?
additional information
?
-
-
possible role of TGase activity in the defense against a viral plant pathogen
-
-
?
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
?
additional information
?
-
-
transglutaminase reactions function in response to mechanical injury. Among the substrates are actin, 40 kDa Ca2+-binding protein CBP40, and a 33 kDa protein highly homologous to the eukaryotic adenine nucleotide translocator
-
-
?
additional information
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
?
additional information
?
-
-
TG2 is related to cell growth at an early stage of liver regeneration after partial hepatectomy, and regulates the growth capacity through down-regulation of the EGF receptor
-
-
?
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides. TG-isoform-specific enzyme activity on rat brain tissue, overview. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides. TG-isoform-specific enzyme activity on rat brain tissue, overview. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
Streptomyces cinnamoneus NBRC 13864
TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
-
-
-
additional information
?
-
-
transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
-
-
-
additional information
?
-
transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
-
-
-
additional information
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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
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additional information
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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
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additional information
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no activity with carbamic acid, thiamine, 2-bromoethylamine, N-ethylmethylamine, sarcosine, butanol, butanethiol, or L-isoleucine methyl ester
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additional information
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transglutaminase catalyzes the acyl transfer reaction between gamma-carboxyamide groups (acyl donor) and primary amines (acyl acceptor). In proteins, it is able to crosslink the gamma-carboxyamide of glutamine and the primary epsilon-amine in lysine
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additional information
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crosslinking activity and IgG reactivity after digestion with cow and horse milk proteins, detailed overview
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microbial transglutaminase (MTG) is a practical tool to enzymatically form isopeptide bonds between peptide or protein substrates. Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements. MTG can react readily with glutamines in alpha-helical, beta-sheet, and unstructured loop elements and does not favor one type of secondary structure. Building of a GB1 library where each variant contains a single glutamine at positions covering all secondary structure elements, detailed overview. The most reactive and selective variants display an over 100fold increase in incorporation compared to another developed aminated benzo[a]imidazo[2,1,5-cd]indolizine-type fluorophore, relative to native GB1
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additional information
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site-specific conjugation to native and engineered lysines in human immunoglobulins by microbial transglutaminase, overview. ESI-MS analysis of antibodies incubated with an acyl donor substrate and enzyme MTG, performed by incubation with ZQG-biotin and MTG at 37°C overnight followed by digestion with IdeS to generate Fab'2 and Fc fragments. A positive-control peptide with two known lysine acyl acceptor sites (GGSTKHKIPGGS) is genetically fused to the C-terminus of mAb1 HC or LC (HC-KTag or LC-KTag, respectively) and analyzed for transamidation. The addition of the KTag to the HC C-terminus blocks removal of Lys447, thereby allowing MTG to utilize Lys447 as an acyl acceptor site. Effect of single C-terminal amino acids on transamidation of HC Lys447, and analysis of transamidation of single lysine substitutions in gamma, iota, kappa, and lambda constant regions, overview. Optimal transamidation of an LC C-terminal lysine requires a spacer between Cys214 and the lysine. Analysis of transamidation of select single lysine substitutions, conducted by incubating samples with ZQG-biotin and MTG at 37°C overnight. Mutational analysis of binding sites
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site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues. Reactivity of IFN alpha-2b to microbial transglutaminase (TGase) allows site-specific conjugation of this protein drug. Production of two monoderivatized isomers of IFN with high yields, mass spectrometry analysis of the two conjugates indicating that they are exclusively modified at the level of Gln101 if the protein is reacted in the presence of an amino-containing ligand (i.e. dansylcadaverine) or at the level of Lys164 if a glutamine-containing molecule is used (i.e. carbobenzoxy-L-glutaminyl-glycine, ZQG). The enzyme is absolutely specific, among the 10 Lys and 12 Gln residues of the protein, only Gln101 and Lys164 are located in highly flexible protein regions
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SM-TAP procession of the pro-form zymogen is not essential for activity as TAMEP-treated and fully processed enzyme and the zymogen exhibit similar catalytic activity
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additional information
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SM-TAP procession of the pro-form zymogen is not essential for activity as TAMEP-treated and fully processed enzyme and the zymogen exhibit similar catalytic activity
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
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the enzymatic transamidation reaction between a gamma-glutamyl donor (Z-Gln-Gly) and hydroxylamine releasing ammonia is coupled to the glutamate dehydrogenase (GDH)-catalyzed reductive amination of 2-oxoglutarate. The activity of GDH is dependent on NADH as a cofactor, whose disappearance can be monitored at 340 nm. NADH concentration was calculated based on a calibration curve, which in turn is used to calculate activity of mTG
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additional information
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the enzyme also catalyzes the deamination of amines. Glutamine is recognised as the acyl donor substrate by TGases due to the gamma-carboxyamide group. N-Benzyloxycarbonyl-L-glutaminylglycine (CBZ-Gln-Gly) is the standard glutamine peptide substrate used for TGases. Acyl acceptor substrates and acyl donor substrates, overview. The mTGase enzyme was reported to recognise L-isomer of lysine slightly more than its D-isomer when incorporated into a Z-Gln-Gly motif
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
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tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
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?
alpha-casein glutamine + alkylamine
alpha-casein N5-alkylglutamine + NH3
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?
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
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?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
beta-crystallin, a major structural protein of the eye lens, is an archetypal TG2 substrate. Its target Gln residue is localized to a peptide sequence denoted A25 (TVQQEL), and is crosslinked to a Lys residue near the C-terminus of the same protein
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