IntEnz

EC 4.2.2.2 - Pectate lyase

IntEnz Enzyme Nomenclature
EC 4.2.2.2

Names

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

Comments:

Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase). Formerly EC 4.2.99.3.

Links to other databases

References

1. Albersheim, P. and Killias, U.
   Studies relating to the purification and properties of pectin transeliminase.
   Arch. Biochem. Biophys. 97: 107-115 (1962). [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: 2403-2408 (1964). [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: 2409-2415 (1964). [PMID: 14235515]
4. Nagel, C.W. and Vaughn, R.H.
   The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa.
   Arch. Biochem. Biophys. 94: 328-332 (1961). [PMID: 13727438]
5. Nasuno, S. and Starr, M.P.
   Polygalacturonic acid trans-eliminase of Xanthomonas campestris.
   Biochem. J. 104: 178-185 (1967). [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: 677-689 (1997). [PMID: 9195887]

[EC 4.2.2.2 created 1965 as EC 4.2.99.3, transferred 1972 to EC 4.2.2.2, modified 2002]