Exo-poly-α-galacturonosidase

Exo-poly-α-galacturonosidase (EC 3.2.1.82, exopolygalacturonosidase, exopolygalacturanosidase, poly(1,4-α-D-galactosiduronate) digalacturonohydrolase) is an enzyme with systematic name poly[(1→4)-α-D-galactosiduronate] digalacturonohydrolase.[1][2][3] It catalyses the hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate.

Exo-poly-α-galacturonosidase
Identifiers
EC no.3.2.1.82
CAS no.37288-58-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

References

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  1. ^ Hasegawa S, Nagel CW (March 1968). "Isolation of an oligogalacturonate hydrolase from a Bacillus specie". Archives of Biochemistry and Biophysics. 124 (1): 513–20. doi:10.1016/0003-9861(68)90360-3. PMID 5661621.
  2. ^ Hatanaka C, Ozawa J (1968). "Enzymic degradation of pectic acid. XIII. New exopolygalacturonase producing digalacturonic acid from pectic acid". J. Agric. Chem. Soc. Jpn. 43: 764–772.
  3. ^ Hatanaka C, Ozawa J (1971). "Unknown". Report of the Ohara Institute for Agricultural Biology. 15: 47. ISSN 0029-0874.
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