| EC |
4.2.2.22 |
| 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 4.2.2.9, 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, KEGG, MetaCyc, PDB |
| References: |
| 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] |
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| [EC 4.2.2.22 created 2007] |
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