β-Agarase
| β-Agarase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.81 | ||||||||
| CAS no. | 37288-57-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Agarase (EC 3.2.1.81, AgaA, AgaB, endo-β-agarase, agarose 3-glycanohydrolase) is an enzyme with systematic name agarose 4-glycanohydrolase. It is found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway.[1] It is responsible for allowing them to use agar as their primary source of carbon and enables their ability to thrive in the ocean.
Agarases are classified as either α-agarases or β-agarases based upon whether they degrade α or β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues.[2]
- ^ Parro V, Mellado RP (1994). "Effect of glucose on agarase overproduction in Streptomyces". Gene. 145 (1): 49–55. doi:10.1016/0378-1119(94)90321-2. PMID 8045423.
- ^ Hassairi I, Ben Amar R, Nonus M, Gupta BB (2001). "Production and separation of α-agarase from Altermonas agarlyticus strain GJ1B". Bioresource Technology. 79 (1): 47–51. Bibcode:2001BiTec..79...47H. doi:10.1016/S0960-8524(01)00037-2. PMID 11396907.