Transglutaminaza
Transglutaminaza je enzim koji katalizuje formiranje kovalentne veze između slobodne amino grupe (e.g., za protein ili peptid vezanog lizina) i gama-karboksamidne grupe proteinskog ili peptidnog glutamina. Ovaj enzim se klasifikuje kao ЕЦ 2.3.2.13. Veze formirane posredstvom transglutaminaze imaju visoku otpornost na proteolitičku degradaciju (proteolizu).
Transglutaminaze su otkrivene 1959.[1] Biohemijsko dejstvo transglutaminaza je otkriveno u krvnom koagulacionom proteinskom faktoru XIII 1968.[2]
Reference уреди
- ^ Clarke DD, Mycek MJ, Neidle A, Waelsch H (1959). „The incorporation of amines into proteins”. Arch Biochem Biophys. 79: 338—354. doi:10.1016/0003-9861(59)90413-8.
- ^ Pisano JJ, Finlayson JS, Peyton MP (1968). „[Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]”. Science. 160 (3830): 892—3. PMID 4967475. doi:10.1126/science.160.3830.892.
Literatura уреди
- Kelleher, James B. (11. 5. 2012). „Industry defends ingredient critics deride as "meat glue"”. Chicago Tribune. Приступљено 20. 7. 2012.
- U.S. Patent 5.156.956 - A transglutaminase catalyzing an acyl transfer reaction of a γ-carboxyamide group of a glutamine residue in a peptide or protein chain in the absence of Cz2+
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
