Glucan 1,4-α-maltotetraohydrolase
Appearance
Glucan 1,4-α-maltotetraohydrolase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.2.1.60 | ||||||||
CAS no. | 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-α-maltotetraohydrolase (EC 3.2.1.60, exo-maltotetraohydrolase, 1,4-α-D-glucan maltotetraohydrolase) is an enzyme with systematic name 4-α-D-glucan maltotetraohydrolase.[1][2] It catalyses the hydrolysis of (1→4)-α-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
References
[edit]- ^ 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 JF, Ackerman RJ (July 1971). "Isolation, purification, and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri". Archives of Biochemistry and Biophysics. 145 (1): 105–14. doi:10.1016/0003-9861(71)90015-4. PMID 5123132.
External links
[edit]- Glucan+1,4-alpha-maltotetraohydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)