KEGG   ENZYME: 4.2.2.10Help
Entry
EC 4.2.2.10                 Enzyme                                 

Name
pectin lyase;
pectin trans-eliminase;
endo-pectin lyase;
polymethylgalacturonic transeliminase;
pectin methyltranseliminase;
pectolyase;
PL;
PNL;
PMGL
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
BRITE hierarchy
Sysname
(1->4)-6-O-methyl-alpha-D-galacturonan lyase
Reaction(IUBMB)
Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends
Comment
Favours pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2, pectate lyase). Demethylation progressively slows its action; it can nevertheless cleave on either side of a demethylated residue if the residue at the other end of the scissile bond is methylated.
History
EC 4.2.2.10 created 1972, modified 2002
Orthology
K01732  
Genes
AFM: 
ANG: 
ANI_1_624124(An14g04370)
ECA: 
ECA1499(pnl)
PSP: 
PSPPH_1424(hopAK1) PSPPH_3992(pnlA)
BSU: 
BSU18650(pelB)
Taxonomy
Reference
1
  Authors
Albersheim, P., Neukom, H. and Deuel, H.
  Title
Uber die Bildung von ungesattigten Abbauprodukten durch ein pekinabbauendes Enzym.
  Journal
Helv. Chim. Acta 43 (1960) 1422-1426.
Reference
2  [PMID:9195887]
  Authors
Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J.
  Title
Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.
  Journal
Structure. 5 (1997) 677-89.
  Organism
Aspergillus niger
  Sequence
Reference
3
  Authors
Kester, H.C.M and Visser, J.
  Title
Purification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger.
  Journal
FEMS Microbiol. Lett. 120 (1994) 63-68.
Reference
4  [PMID:12110197]
  Authors
Mutenda KE, Korner R, Christensen TM, Mikkelsen J, Roepstorff P.
  Title
Application of mass spectrometry to determine the activity and specificity of pectin lyase A.
  Journal
Carbohydr. Res. 337 (2002) 1217-27.
  Organism
Aspergillus niger
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9033-35-6

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