| EC |
4.2.2.2 |
| Accepted name: |
pectate lyase |
| Reaction: |
Eliminative cleavage of (1→4)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends |
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For diagram of reaction, click here |
| Other name(s): |
polygalacturonic transeliminase; pectic acid transeliminase; polygalacturonate lyase; endopectin methyltranseliminase; pectate transeliminase; endogalacturonate transeliminase; pectic acid lyase; pectic lyase; α-1,4-D-endopolygalacturonic acid lyase; PGA lyase; PPase-N; endo-α-1,4-polygalacturonic acid lyase; polygalacturonic acid lyase; pectin trans-eliminase; Polygalacturonic acid trans-eliminase |
| Systematic name: |
(1→4)-α-D-galacturonan lyase |
| Comments: |
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9015-75-2 |
| References: |
| 1. |
Albersheim, P. and Killias, U. Studies relating to the purification and properties of pectin transeliminase. Arch. Biochem. Biophys. 97 (1962) 107–115. [DOI] [PMID: 13860094] |
| 2. |
Edstrom, R.D. and Phaff, H.J. Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus. J. Biol. Chem. 239 (1964) 2403–2408. [PMID: 14235514] |
| 3. |
Edstrom, R.D. and Phaff, H.J. Eliminative cleavage of pectin and of oligogalacturonide methyl esters by pectin trans-eliminase. J. Biol. Chem. 239 (1964) 2409–2415. [PMID: 14235515] |
| 4. |
Nagel, C.W. and Vaughn, R.H. The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa. Arch. Biochem. Biophys. 94 (1961) 328. [DOI] [PMID: 13727438] |
| 5. |
Nasuno, S. and Starr, M.P. Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J. 104 (1967) 178–185. [PMID: 6035509] |
| 6. |
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. [DOI] [PMID: 9195887] |
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| [EC 4.2.2.2 created 1965 as EC 4.2.99.3, transferred 1972 to EC 4.2.2.2, modified 2002] |
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