Glucan 1,4-alpha-maltotetraohydrolase
| Glucan 1,4-alpha-maltotetraohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.60 | ||||||||
| CAS number | 37288-44-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glucan 1,4-alpha-maltotetraohydrolase (EC 3.2.1.60, exo-maltotetraohydrolase, 1,4-alpha-D-glucan maltotetraohydrolase) is an enzyme with systematic name 4-alpha-D-glucan maltotetraohydrolase.[1][2] This enzyme catalyses the following chemical reaction
- Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
References
- ↑ Nakakuki, T.; Azuma, K.; Kainuma, K. (1984). "Action patterns of various exo-amylases and the anomeric configurations of their products". Carbohydr. Res. 128: 297–310. doi:10.1016/0008-6215(84)85337-9.
- ↑ Robyt, J.F.; Ackerman, R.J. (1971). "Isolation, purification, and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri". Arch. Biochem. Biophys. 145: 105–114. doi:10.1016/0003-9861(71)90015-4. PMID 5123132.
External links
- Glucan+1,4-alpha-maltotetraohydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from
Wikipedia.
The text is licensed under Creative Commons - Attribution - Sharealike.
Additional terms may apply for the media files.