Gellan lyase
| Gellan lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.25 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Gellan lyase (EC 4.2.2.25) is an enzyme with systematic name gellan beta-D-glucopyranosyl-(1->4)-D-glucopyranosyluronate lyase.[1][2][3] This enzyme catalyses the following chemical reaction
- Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end.
The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp.
References
- ^ Hashimoto W, Maesaka K, Sato N, Kimura S, Yamamoto K, Kumagai H, Murata K (March 1997). "Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1". Archives of Biochemistry and Biophysics. 339 (1): 17–23. doi:10.1006/abbi.1996.9851. PMID 9056228.
- ^ Hashimoto W, Sato N, Kimura S, Murata K (June 1998). "Polysaccharide lyase: molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1". Archives of Biochemistry and Biophysics. 354 (1): 31–9. doi:10.1006/abbi.1998.0674. PMID 9633595.
- ^ Miyake O, Kobayashi E, Nankai H, Hashimoto W, Mikami B, Murata K (February 2004). "Posttranslational processing of polysaccharide lyase: maturation route for gellan lyase in Bacillus sp. GL1". Archives of Biochemistry and Biophysics. 422 (2): 211–20. doi:10.1016/j.abb.2003.12.015. PMID 14759609.
External links
- Gellan+lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
