Mechanism and BASIS for Specificity of Transglutaminase‐Catalyzed ε‐(γ‐Glutamyl) Lysine Bond Formation

Folk, J.E.

doi:10.1002/9780470122990.ch1

Cited by 146 publications

(110 citation statements)

References 67 publications

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“…TGases were first described as enzymes that facilitate the formation of N-ε (γ-glutamyl)lysine isopeptide bond between endo-γ-glutaminyl and endo-ε-lysyl protein residues, or the covalent incorporation of diamines and polyamines in proteins (Folk 1983). Scarnato et al (2016) focus on the effects of TGases and sourdough on protein profiles and volatile molecules of gluten free dough.…”

Section: Editorialmentioning

confidence: 99%

Polyamines and transglutaminases: future perspectives

Agostinelli

2016

Amino Acids

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Section: Editorialmentioning

confidence: 99%

Polyamines and transglutaminases: future perspectives

Agostinelli

2016

Amino Acids

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“…They are also widely present in most animal tissues and body fluids (Folk 1983;Lorand & Conrad 1984). TGases have been discovered in microorganisms including Candida albicans (Ruiz-Herrera et al 1995), Bacillus subtilis (Kobayashi et al 1996), Escherichia coli (Schmidt et al 1998), Physarum polycephalum (Klein et al 1992), and actinomycetes (Kanaji et al 1993;Gerber et al 1994;Duran et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Optimization of transconjugation and characterization of attB integration site for Streptomyces cinnamoneus producing transglutaminase

Park

Choi

2014

Biologia

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An effective transformation method for molecular genetic studies of Streptomyces cinnamoneus producing transglutaminase was established using intergeneric conjugal transfer based on the bacteriophage ΦC31 att/int system. The high efficiency of S. cinnamoneus transconjugation was obtained on mannitol soya flour medium containing 50 mM MgCl2, using 2.5 × 10 8 Escherichia coli as donor and spores treated with heat treatment at 35• C for 10 min as host. By cloning and sequencing the attB integration site, a single attB site within an open reading frame coding for a pirin homologue was located in S. cinnamoneus genome. Its sequence exhibited the highest degree of sequence similarity with that of Streptomyces clavuligerus. These results provide sufficient efficiency to enable conjugal transfer of genetic elements for S. cinnamoneus, and also should facilitate molecular genetic studies for improvement in production ability of transglutaminase used in food industry.

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“…2.3.2.13, protein-glutamine c-glutamyltransferase) gene family, known to catalyze both inter-and intra-molecular isopeptide bonds between specific glutamine c-carboxamide groups and e-amino groups in Lys and free primary amines (TGase). [1][2][3] The crosslinking reaction functions to promote extracellular matrix stabilization and wound healing; however, abnormal crosslinking contributes to tissue fibrosis and several neurodegenerative diseases including Huntington's, Parkinson's, and Alzheimer's diseases. 4 TGM2 was validated as a therapeutic target in expanded polyQ diseases based on evidence from TGM2 knock-out experiments 5,6 and TGM2 inhibition studies.…”

Section: Introductionmentioning

confidence: 99%

Human tissue transglutaminase is inhibited by pharmacologic and chemical acetylation

2010

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Human tissue transglutaminase (TGM2) is implicated in the pathogenesis of several neurodegenerative disorders including Alzheimer's, Parkinson's and expanded polyglutamine (polyQ) diseases. TGM2 promotes formation of soluble and insoluble high molecular weight aggregates by catalyzing a covalent linkage between peptide-bound Q residues in polyQ proteins and a peptide-bound Lys residue. Therapeutic approaches to modulate the activity of TGM2 are needed to proceed with studies to test the efficacy of TGM2 inhibition in disease processes. We investigated whether acetylation of Lys-residues by sulfosuccinimidyl acetate (SNA) or aspirin (ASA) would alter the crosslinking activity of TGM2. Acetylation by either SNA and/or ASA resulted in a loss of >90% of crosslinking activity. The Lys residues that were critical for inhibition were identified by mass spectrometry as Lys . Hence, acetylation of Lys-residues may modulate the enzymatic function of TGM2 in vivo and offer a novel approach to treatment of TGM2 mediated disorders.

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Mechanism and BASIS for Specificity of Transglutaminase‐Catalyzed ε‐(γ‐Glutamyl) Lysine Bond Formation

Cited by 146 publications

References 67 publications

Polyamines and transglutaminases: future perspectives

Polyamines and transglutaminases: future perspectives

Optimization of transconjugation and characterization of attB integration site for Streptomyces cinnamoneus producing transglutaminase

Human tissue transglutaminase is inhibited by pharmacologic and chemical acetylation

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