Pectate trisaccharide-lyase

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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

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[edit]

  1. ^ Kluskens, L.D.; van Alebeek, G.J.; Voragen, A.G.; de Vos, W.M.; 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. PMC 1223193Freely accessible. PMID 12443532. 
  2. ^ Tamaru, Y.; 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. PMC 31190Freely accessible. PMID 11259664. 
  3. ^ Berensmeier, S.; Singh, S.A.; Meens, J.; 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. 

External links[edit]