Pectate trisaccharide-lyase (EC 4.2.2.22 , exopectate-lyase , pectate lyase A , PelA ) is an enzyme with systematic name (1→4)-α-D -galacturonan reducing-end-trisaccharide-lyase . This enzyme catalyses the following chemical reaction :
eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid /pectate
The predominant action of this enzyme is removal of a trisaccharide .
References
Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM, van der Oost J (March 2003). "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima" . The Biochemical Journal . 370 (Pt 2): 651–9. doi :10.1042/bj20021595 . PMC 1223193 . PMID 12443532 .
Tamaru Y, Doi RH (March 2001). "Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome" . Proceedings of the National Academy of Sciences of the United States of America . 98 (7): 4125–9. doi :10.1073/pnas.071045598 . PMC 31190 . PMID 11259664 .
Berensmeier S, Singh SA, Meens J, Buchholz K (May 2004). "Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase". Applied Microbiology and Biotechnology . 64 (4): 560–7. doi :10.1007/s00253-003-1446-9 . PMID 14673544 . S2CID 23236787 .
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Enzymes Activity
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Pectate trisaccharide-lyase
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