Endo-1,3(4)-β-glucanase

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Endo-1,3(4)-β-glucanase
Identifiers
EC no.3.2.1.6
CAS no.62213-14-3
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Endo-1,3(4)-β-glucanase (EC 3.2.1.6, endo-1,3-β-D-glucanase, laminarinase, β-1,3-glucanase,4-glucanase, endo-β-(1→3)-D-glucanase, endo-1,3-1,4-β-D-glucanase, endo-β-(1-3)-D-glucanase, endo-β-1,3-glucanase IV, 1,3-1,4)-β-D-glucan 3(4)-glucanohydrolase) is an enzyme with systematic name 3(or 4)-β-D-glucan 3(4)-glucanohydrolase.[1][2][3][4][5] It catalyses the following chemical reaction

Endohydrolysis of (1→3)- or (1→4)-linkages in β-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 DR, Stone BA (November 1969). "β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases". Biochimica et Biophysica Acta (BBA) - Enzymology. 191 (2): 329–41. doi:10.1016/0005-2744(69)90252-6. PMID 5354264.
  2. ^ Barras DR, Stone BA (November 1969). "β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase". Biochimica et Biophysica Acta (BBA) - Enzymology. 191 (2): 342–53. doi:10.1016/0005-2744(69)90253-8. PMID 5354265.
  3. ^ Cunningham LW, Manners DJ (1961). "Enzymic degradation of lichenin". Biochem. J. 80: 42.
  4. ^ Reese ET, Mandels M (April 1959). "β-D-1,3 Glucanases in fungi". Canadian Journal of Microbiology. 5 (2): 173–85. doi:10.1139/m59-022. PMID 13638895.
  5. ^ Sova VV, Elyakova LA, Vaskovsky VE (July 1970). "Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis". Biochimica et Biophysica Acta (BBA) - Enzymology. 212 (1): 111–5. doi:10.1016/0005-2744(70)90183-X. PMID 5500926.

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