Pectate trisaccharide-lyase
| Pectate trisaccharide-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.22 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pectate trisaccharide-lyase (EC 4.2.2.22, exopectate-lyase, pectate lyase A, PelA) is an enzyme with system name (1->4)-alpha-D-galacturonan reducing-end-trisaccharide-lyase.[1][2][3] 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, L.D., van Alebeek, G.J., Voragen, A.G., de Vos, W.M. and van der Oost, J. (2003). "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima". Biochem. J. 370: 651–659. doi:10.1042/bj20021595. PMID 12443532.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Tamaru, Y. and Doi, R.H. (2001). "Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome". Proc. Natl. Acad. Sci. USA. 98: 4125–4129. doi:10.1073/pnas.071045598. PMID 11259664.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Berensmeier, S., Singh, S.A., Meens, J. and Buchholz, K. (2004). "Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase". Appl. Microbiol. Biotechnol. 64: 560–567. doi:10.1007/s00253-003-1446-9. PMID 14673544.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Pectate+trisaccharide-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)