Endo-1,3(4)-b-glucanase

Endo-1,3(4)-beta-glucanase
Identifiers
EC number 3.2.1.6
CAS number 62213-14-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Endo-1,3(4)-beta-glucanase (EC 3.2.1.6, endo-1,3-beta-D-glucanase, laminarinase, beta-1,3-glucanase, beta-1,3-1,4-glucanase, endo-1,3-beta-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-(1->3)-D-glucanase, endo-1,3-1,4-beta-D-glucanase, endo-beta-(1-3)-D-glucanase, endo-beta-1,3-glucanase IV, 1,3-(1,3, 1,4)-beta-D-glucan 3(4)-glucanohydrolase) is an enzyme with systematic name 3(or 4)-beta-D-glucan 3(4)-glucanohydrolase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3

Substrates include laminarin, lichenin and cereal D-glucans.

References

  1. ↑ Barras, D.R.; Stone, B.A. (1969). "β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases". Biochim. Biophys. Acta. 191 (2): 329–341. PMID 5354264. doi:10.1016/0005-2744(69)90252-6.
  2. ↑ Barras, D.R.; Stone, B.A. (1969). "β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase". Biochim. Biophys. Acta. 191 (2): 342–353. PMID 5354265. doi:10.1016/0005-2744(69)90253-8.
  3. ↑ Cunningham, L.W.; Manners, D.J. (1961). "Enzymic degradation of lichenin". Biochem. J. 80: 42–42.
  4. ↑ Reese, E.T.; Mandels, M. (1959). "β-D-1,3-Glucanases in fungi". Can. J. Microbiol. 5 (2): 173–185. PMID 13638895. doi:10.1139/m59-022.
  5. ↑ Sova, V.V.; Elyakova, L.A.; Vaskovsky, V.E. (1970). "Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis". Biochim. Biophys. Acta. 212 (1): 111–115. PMID 5500926. doi:10.1016/0005-2744(70)90183-X.
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