Protein modification by transglutaminase
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Accession number;05A0630947
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| Title;Protein modification by transglutaminase |
| Author;
HITOMI KIYOTAKA
(Nagoya Univ., Graduate School of Bioagricultural Sci., JPN)
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Journal Title;Seikagaku
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Journal Code:G0184A
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ISSN:0037-1017
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VOL.77;NO.6;PAGE.552-558(2005)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;This article introduces the post-translational modification of protein by "protein", which takes place in a reaction catalyzed by an enzyme called transglutaminase. In this enzymatic reaction, a glutamyl residue of a protein substrate is cross-linked with a lysil residue of a different protein or the same protein by a stable covalent bond. There are also cases where a glutamyl reside of certain substrates binds with a primary amine or undergoes deacylation to glutamic acid. Such cross-linking and modification reaction bring about alterations in biochemical properties of a protein including functions and solubility. This enzymatic reaction in animals is calcium-dependent, proceeds by extracellualr stimulation, and is involved in various phenomena such as body construction in surface layer, cell death, signal transmmission, and so on. In addition to normal physiological functions. it is also involved in various events; it is even involved as a cause of disease state. An introduction is given with a focus on these cases. (Author's abstract). |
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