The Enzyme Database

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Accepted name: pectate trisaccharide-lyase
Reaction: eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
Other name(s): exopectate-lyase; pectate lyase A; PelA
Systematic name: (1→4)-α-D-galacturonan reducing-end-trisaccharide-lyase
Comments: Differs in specificity from EC, pectate disaccharide-lyase, as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end. Disaccharides and tetrasaccharides may also be removed [2].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Kluskens, L.D., van Alebeek, G.J., Voragen, A.G., de Vos, W.M. and van der Oost, J. Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima. Biochem. J. 370 (2003) 651–659. [DOI] [PMID: 12443532]
2.  Tamaru, Y. and Doi, R.H. Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome. Proc. Natl. Acad. Sci. USA 98 (2001) 4125–4129. [DOI] [PMID: 11259664]
3.  Berensmeier, S., Singh, S.A., Meens, J. and Buchholz, K. Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase. Appl. Microbiol. Biotechnol. 64 (2004) 560–567. [DOI] [PMID: 14673544]
[EC created 2007]

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