EC 4.2.2.2 - Pectate lyase
IntEnz view
ENZYME view
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
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
- Eliminative cleavage of (1right4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Gene Ontology:
GO:0030570
CAS Registry Number:
9015-75-2
References
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Studies relating to the purification and properties of pectin transeliminase.Arch. Biochem. Biophys. 97 : 107-115 (1962). [PMID: 13860094]
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Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus.J. Biol. Chem. 239 : 2403-2408 (1964). [PMID: 14235514]
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Eliminative cleavage of pectin and of oligogalacturonide methyl esters by pectin trans-eliminase.J. Biol. Chem. 239 : 2409-2415 (1964). [PMID: 14235515]
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The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa.Arch. Biochem. Biophys. 94 : 328-332 (1961). [PMID: 13727438]
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Polygalacturonic acid trans-eliminase of Xanthomonas campestris.Biochem. J. 104 : 178-185 (1967). [PMID: 6035509]
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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]