Biology:Pectate trisaccharide-lyase
From HandWiki
| Pectate trisaccharide-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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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.[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
- ↑ "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. March 2003. doi:10.1042/bj20021595. PMID 12443532.
- ↑ "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. March 2001. doi:10.1073/pnas.071045598. PMID 11259664.
- ↑ "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. May 2004. doi:10.1007/s00253-003-1446-9. PMID 14673544.
External links
- Pectate+trisaccharide-lyase at the US National Library of Medicine Medical Subject Headings (MeSH)
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