Jump to content

Gellan lyase

From Wikipedia, the free encyclopedia
Gellan lyase
Identifiers
EC no.4.2.2.25
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Gellan lyase (EC 4.2.2.25) is an enzyme with systematic name gellan β-D-glucopyranosyl-(1→4)-D-glucopyranosyluronate lyase.[1][2][3] This enzyme catalyses the following process:

Eliminative cleavage of β-D-glucopyranosyl-(1→4)-β-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 β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-DGlcp-(1→4)-α-L-Rhap-(1→3)-β-D-Glcp.

References

[edit]
  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
[edit]