KEGG   ENZYME: 4.2.2.22
Entry
EC 4.2.2.22                 Enzyme                                 
Name
pectate trisaccharide-lyase;
exopectate-lyase;
pectate lyase A;
PelA
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
Sysname
(1->4)-alpha-D-galacturonan reducing-end-trisaccharide-lyase
Reaction(IUBMB)
eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate
Comment
Differs in specificity from EC 4.2.2.9, pectate disaccharide-lyase, as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end. Disaccharides and tetrasaccharides may also be removed [2].
History
EC 4.2.2.22 created 2007
Reference
1  [PMID:12443532]
  Authors
Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM, van der Oost J
  Title
Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima.
  Journal
Biochem J 370:651-9 (2003)
DOI:10.1042/BJ20021595
  Sequence
[tma:TM0433]
Reference
2  [PMID:11259664]
  Authors
Tamaru Y, Doi RH.
  Title
Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome.
  Journal
Proc Natl Acad Sci U S A 98:4125-9 (2001)
DOI:10.1073/pnas.071045598
Reference
3  [PMID:14673544]
  Authors
Berensmeier S, Singh SA, Meens J, Buchholz K.
  Title
Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase.
  Journal
Appl Microbiol Biotechnol 64:560-7 (2004)
DOI:10.1007/s00253-003-1446-9
  Sequence
[bld:BLi04129]
Other DBs
ExplorEnz - The Enzyme Database: 4.2.2.22
IUBMB Enzyme Nomenclature: 4.2.2.22
ExPASy - ENZYME nomenclature database: 4.2.2.22
BRENDA, the Enzyme Database: 4.2.2.22

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