EC 4.2.2.2 - Pectate lyase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 4.2.2.2

Names

Accepted name:
pectate lyase
Other names:
α-1,4-D-endopolygalacturonic acid lyase
PGA lyase
PPase-N
polygalacturonic acid trans-eliminase
endo-α-1,4-polygalacturonic acid lyase
endogalacturonate transeliminase
endopectin methyltranseliminase
pectate transeliminase
pectic acid lyase
pectic acid transeliminase
pectic lyase
pectin trans-eliminase
polygalacturonate lyase
polygalacturonic acid lyase
polygalacturonic transeliminase
Systematic name:
(1→4)-α-D-galacturonan lyase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0030570
CAS Registry Number: 9015-75-2
UniProtKB/Swiss-Prot: (110) [show] [UniProt]

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]