Alpha-agarase
| Alpha-agarase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.158 | ||||||||
| CAS number | 63952-00-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alpha-agarase (EC 3.2.1.158, agarase, agaraseA33) is an enzyme with system name agarose 3-glycanohydrolase.[1][2] This enzyme catalyses the following chemical reaction
- Endohydrolysis of (1->3)-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product
This enzyme requires Ca2+.
References
- ↑ Potin, P., Richard, C., Rochas, C. and Kloareg, B. (1993). "Purification and characterization of the α-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B". Eur. J. Biochem. 214: 599–607. doi:10.1111/j.1432-1033.1993.tb17959.x. PMID 8513809.
- ↑ Ohta, Y., Hatada, Y., Miyazaki, M., Nogi, Y., Ito, S. and Horikoshi, K. (2005). "Purification and characterization of a novel α-agarase from a Thalassomonas sp". Curr. Microbiol. 50: 212–216. doi:10.1007/s00284-004-4435-z. PMID 15902469.
External links
- Alpha-agarase at the US National Library of Medicine Medical Subject Headings (MeSH)