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DeutschAlpha-agarase
| Alpha-agarase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.158 | ||||||||
| CAS no. | 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 systematic 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
[edit]- ^ Potin P, Richard C, Rochas C, Kloareg B (June 1993). "Purification and characterization of the alpha-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B". European Journal of Biochemistry. 214 (2): 599–607. doi:10.1111/j.1432-1033.1993.tb17959.x. PMID 8513809.
- ^ Ohta Y, Hatada Y, Miyazaki M, Nogi Y, Ito S, Horikoshi K (April 2005). "Purification and characterization of a novel alpha-agarase from a Thalassomonas sp". Current Microbiology. 50 (4): 212–6. doi:10.1007/s00284-004-4435-z. PMID 15902469.
External links
[edit]- Alpha-agarase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
