Accession NumberHMDB03869
Common_Nameepsilon-(gamma-Glutamyl)-lysine
DescriptionIn non-diabetic kidney scarring the protein crosslinking enzyme tissue transglutaminase (tTg) has been implicated in the process by the formation of increased epsilon-(gamma-glutamyl)lysine bonds between ECM components in both experimental and human disease. Changes in tTg and epsilon-(gamma-glutamyl)lysine occur in human Diabetic nephropathy as well, the leading cause of chronic kidney failure. (PMID 15292688) In Parkinson's disease (PD), conformational changes in the alpha-synuclein monomer precede the formation of Lewy bodies. Both tTG and its substrate-characteristic N(epsilon)-(gamma-glutamyl)-lysine crosslink are increased in PD nigral dopamine neurons. (PMID 15001552) Expression of tissue transglutaminase (tTgase) and epsilon-(gamma-glutamyl)-lysine was present in all scarring of the blebs sites, being the main cause of failure in glaucoma filtration surgery. Transglutaminases are calcium-dependent enzymes that catalyze the posttranslational modification of proteins through an acyl transfer reaction between the gamma-carboxamide group of a peptide-bound glutaminyl residue and various amines. Covalent cross-linking using epsilon-(gamma-glutamyl)-lysine bonds is stable and resistant to enzymatic, chemical, and mechanical disruption. (PMID: 16936095)
Chemical_IUPAC_Name(2S)-6-amino-2-[[(4S)-4-amino-4-carboxy-butanoyl]amino]hexanoic acid
Chemical FormulaC11H21N3O5
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