(1-4)-alpha-D-galacturonan reducing-end-trisaccharide-lyase

Pectate trisaccharide-lyase
Identifiers
EC number4.2.2.22
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Pectate trisaccharide-lyase (EC 4.2.2.22, exopectate-lyase, pectate lyase A, PelA) is an enzyme with systematic 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[]

  1. ^ Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM, van der Oost J (March 2003). "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. doi:10.1042/bj20021595. PMC 1223193. PMID 12443532.
  2. ^ Tamaru Y, Doi RH (March 2001). "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. doi:10.1073/pnas.071045598. PMC 31190. PMID 11259664.
  3. ^ Berensmeier S, Singh SA, Meens J, Buchholz K (May 2004). "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. doi:10.1007/s00253-003-1446-9. PMID 14673544.

External links[]