The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 4.2.2.10     
Accepted name: pectin lyase
Reaction: Eliminative cleavage of (1→4)-α-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-α-D-galact-4-enuronosyl groups at their non-reducing ends
For diagram of reaction, click here
Other name(s): pectin trans-eliminase; endo-pectin lyase; polymethylgalacturonic transeliminase; pectin methyltranseliminase; pectolyase; PL; PNL; PMGL
Systematic name: (1→4)-6-O-methyl-α-D-galacturonan lyase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-35-6
References:
1.  Albersheim, P., Neukom, H. and Deuel, H. Über die Bildung von ungesättigten Abbauprodukten durch ein pekinabbauendes Enzym. Helv. Chim. Acta 43 (1960) 1422–1426.
2.  Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. 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. Structure 5 (1997) 677–689. [PMID: 9195887]
3.  Kester, H.C.M and Visser, J. Purification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger. FEMS Microbiol. Lett. 120 (1994) 63–68.
4.  Mutenda, K.E., Körner, R., Christensen, T.M.I.E., Mikkelsen, J. and Roepstorff, P. Application of mass spectrometry to determine the activity and specificity of pectin lyase A. Carbohydr. Res. 337 (2002) 1213–1223. [PMID: 12110197]
[EC 4.2.2.10 created 1972, modified 2002]
 
 


Data © 2001–2014 IUBMB
Web site © 2005–2014 Andrew McDonald