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== External links ==
== External links ==
* {{MeshName|Pectate+trisaccharide-lyase}}
* {{MeshName|Pectate+trisaccharide-lyase}}

{{Carbon-oxygen lyases}}


[[Category:EC 4.2.2]]
[[Category:EC 4.2.2]]

Revision as of 16:15, 31 January 2016

Pectate trisaccharide-lyase
Identifiers
EC no.4.2.2.22
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

  1. ^ 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)
  2. ^ 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)
  3. ^ 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