Beta-porphyranase
| Beta-porphyranase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.178 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Beta-porphyranase (EC 3.2.1.178, porphyranase, PorA, PorB, endo-beta-porphyranase) is an enzyme with systematic name porphyran beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate 4-glycanohydrolase.[1][2] This enzyme catalyses the following chemical reaction
- Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran
The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate.
References
- ↑ Hehemann, J.H.; Correc, G.; Barbeyron, T.; Helbert, W.; Czjzek, M.; Michel, G. (2010). "Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota". Nature. 464: 908–912. doi:10.1038/nature08937. PMID 20376150.
- ↑ Correc, G.; Hehemann, J.H.; Czjzek, M.; Helbert, W. (2011). "Structural analysis of the degradation products of porphyran digested by Zobellia galactanivorans β-porphyranase A". Carbohydrate Polymers. 83: 277–283. doi:10.1016/j.carbpol.2010.07.060.
External links
- Beta-porphyranase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/16/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.