Pectate disaccharide-lyase
| pectate disaccharide-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.9 | ||||||||
| CAS no. | 37290-87-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a pectate disaccharide-lyase (EC 4.2.2.9) is an enzyme that catalyzes the chemical reaction
- Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is (1->4)-alpha-D-galacturonan reducing-end-disaccharide-lyase. Other names in common use include pectate exo-lyase, exopectic acid transeliminase, exopectate lyase, exopolygalacturonic acid-trans-eliminase, PATE, exo-PATE, and exo-PGL.
References
- Macmillan JD; Vaughn RH (1964). "Purification and properties of a polygalacturonic acid-trans-eliminase produced by Clostridium multifermentans". Biochemistry. 3 (4): 564–572. doi:10.1021/bi00892a016. PMID 14188174.