| Exo-poly-α-galacturonosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.82 | ||||||||
| CAS no. | 37288-58-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.
References
- ^ 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.
- ^ 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.
- ^ Hatanaka C, Ozawa J (1971). "Unknown". Report of the Ohara Institute for Agricultural Biology. 15: 47. ISSN 0029-0874.
External links
- Exo-poly-alpha-galacturonosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Exo-poly-α-galacturonosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.82 | ||||||||
| CAS no. | 37288-58-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.
References
- ^ 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.
- ^ 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.
- ^ Hatanaka C, Ozawa J (1971). "Unknown". Report of the Ohara Institute for Agricultural Biology. 15: 47. ISSN 0029-0874.
External links
- Exo-poly-alpha-galacturonosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)