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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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ApoE glutamine + alkylamine
ApoE 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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casein glutamine + alkylamine
casein N5-alkylglutamine + NH3
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CBP40 + ?
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a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
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Cbz-Gln-Gly + alkylamine
Cbz-Glu-Gly + NH3
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Cbz-L-Gln-Gly + alkylamine
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collagen glutamine + alkylamine
collagen N5-alkylglutamine + NH3
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cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
cornifin-A is SPR1
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desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
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epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
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fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
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fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
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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
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gelatin glutamine + alkylamine
gelatin N5-alkylglutamine + NH3
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gliadin glutamine + alkylamine
gliadin N5-alkylglutamine + NH3
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hornein glutamine + pentylamine
hornein N5-pentylglutamine + NH3
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involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
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junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
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kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
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leishmanolysin + alkylamine
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myo-inositol-1-phosphate synthase + alkylamine
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N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
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N,N-dimethylcasein + putrescine
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N-acetyl-PNPQLPF + alkylamine
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N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
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specific high-affinity substrate
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N-carboxybenzoyl-L-glutaminylglycine + alkylamine
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N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
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Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
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plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
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plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
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preferred substrate
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pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
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pollen cell-wall protein + N,N-dimethylcasein
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protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein-bound gamma-glutamine + putrescine
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SPR2D glutamine + pentylamine
SPR2D N5-pentylglutamine + NH3
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thylakoid protein + putrescine
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the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
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transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
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[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
additional information
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N-carboxybenzoyl-L-glutaminylglycine + alkylamine
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N-carboxybenzoyl-L-glutaminylglycine + alkylamine
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protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
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protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
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protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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transglutaminase is probably involved in cell death program
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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mediates membrane-structural changes
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitor to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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epidermal enzyme involved in formation of cornified envelope
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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epidermal enzyme involved in formation of cornified envelope
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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actin is probably the major endogenous substrate
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protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
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additional information
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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
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additional information
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enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
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additional information
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enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
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additional information
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enzyme may be involved in cataractogenesis
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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several substrate candidates of TG1 that may be essential for cornified envelope formation are identified and characterized
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additional information
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major substrates of enzyme are in the range of 50-75 kDA
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additional information
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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
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additional information
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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
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additional information
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hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
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additional information
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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
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additional information
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enzyme is related with the first wave of spermatogenesis
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additional information
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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
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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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tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
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