| EC |
3.2.1.82 |
| Accepted name: |
exo-poly-α-digalacturonosidase |
| Reaction: |
[(1→4)-α-D-galacturonosyl]n + H2O = α-D-galacturonosyl-(1→4)-D-galacturonate + [(1→4)-α-D-galacturonosyl]n-2 |
| Other name(s): |
pehX (gene name); poly(1,4-α-D-galactosiduronate) digalacturonohydrolase; exopolygalacturonosidase (misleading); poly[(1→4)-α-D-galactosiduronate] digalacturonohydrolase; exo-poly-α-galacturonosidase |
| Systematic name: |
poly[(1→4)-α-D-galactosiduronate] non-reducing-end-digalacturonohydrolase |
| Comments: |
The enzyme, characterized from bacteria, hydrolyses the second α-1,4-glycosidic bond from the non-reducing end of polygalacturonate, releasing digalacturonate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-58-7 |
| References: |
| 1. |
Hasegawa, H. and Nagel, C.W. Isolation of an oligogalacturonate hydrolase from a Bacillus species. Arch. Biochem. Biophys. 124 (1968) 513–520. [DOI] [PMID: 5661621] |
| 2. |
Hatanaka, C. and Ozawa, J. Enzymic degradation of pectic acid. XIII. New exopolygalacturonase producing digalacturonic acid from pectic acid. J. Agric. Chem. Soc. Jpn.. 43 (1968) 764–772. |
| 3. |
Hatanaka, C. and Ozawa, J. Ber. des O'Hara Inst. 15 (1971) 47. |
| 4. |
He, S.Y. and Collmer, A. Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-α-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16. J. Bacteriol. 172 (1990) 4988–4995. [PMID: 2168372] |
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| [EC 3.2.1.82 created 1972, modified 2019] |
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