EC 3 - Hydrolases
EC 3.2 - Glycosylases
EC 3.2.1 - Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
EC 3.2.1.67 - Galacturonan 1,4-α-galacturonidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.2.1.67
Names
Accepted name:
galacturonan 1,4-α-galacturonidase
Other
names:
exo-D-galacturonanase
exo-D-galacturonase
exopoly-D-galacturonase
exopolygalacturonase
poly(galacturonate) hydrolase [ambiguous]
poly(1,4-α-D-galacturonide) galacturonohydrolase [ambiguous]
pgaA (gene name)
galacturan 1,4-α-galacturonidase [incorrect]
exo-D-galacturonase
exopoly-D-galacturonase
exopolygalacturonase
poly(galacturonate) hydrolase [ambiguous]
poly(1,4-α-D-galacturonide) galacturonohydrolase [ambiguous]
pgaA (gene name)
galacturan 1,4-α-galacturonidase [incorrect]
Systematic name:
poly[(1→4)-α-D-galacturonide] non-reducing-end galacturonohydrolase
Reaction
-
14117 [IUBMB][(1→4)-α-D-galacturonosyl](n)POLYMER:14570Formula: H2O(C6H7O6)n
Charge: (0)(-1)nH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)=[(1→4)-α-D-galacturonosyl](n-1)POLYMER:14572Formula: H2O(C6H7O6)n-1
Charge: (0)(-1)n-1
Comments:
The enzyme hydrolyses the first glycosidic bond from the non-reducing end of the substrate. It is specific for saturated oligomers of D-homogalacturonan, and is unable to degrade unsaturated substrates or methyl-esterified substrates.
Links to other databases
Protein domains and families:
PROSITE:PDOC00415
Gene Ontology:
GO:0047911
CAS Registry Number:
9045-35-6
References
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Isolation of an oligogalacturonate hydrolase from a Bacillus species.Arch. Biochem. Biophys. 124 : 513-520 (1968). [PMID: 5661621]
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Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima.FEBS J. 272 : 5464-5473 (2005). [PMID: 16262687]
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A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation.Biochem. J. 400 : 43-52 (2006). [PMID: 16822232]
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The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer.FEBS Lett. 583 : 3665-3670 (2009). [PMID: 19854184]
[EC 3.2.1.67 created 1972, modified 2019]